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Carsten Krebs - Publications

Affiliations: 
Pennsylvania State University, State College, PA, United States 
Area:
Biochemistry
Website:
http://sites.psu.edu/bollingerkrebsgroup/carsten-krebs/
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199 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2024 Burke EJ, Copeland RA, Dixit Y, Krebs C, Bollinger JM. Steric Perturbation of the Grob-like Final Step of Ethylene-Forming Enzyme Enables 3-Hydroxypropionate and Propylene Production. Journal of the American Chemical Society. 146: 1977-1983. PMID 38226594 DOI: 10.1021/jacs.3c09733  0.75
2023 Maio N, Raza MK, Li Y, Zhang DL, Bollinger JM, Krebs C, Rouault TA. An iron-sulfur cluster in the zinc-binding domain of the SARS-CoV-2 helicase modulates its RNA-binding and -unwinding activities. Proceedings of the National Academy of Sciences of the United States of America. 120: e2303860120. PMID 37552760 DOI: 10.1073/pnas.2303860120  0.719
2023 Slater JW, Lin CY, Neugebauer ME, McBride MJ, Sil D, Nair MA, Katch BJ, Boal AK, Chang MCY, Silakov A, Krebs C, Bollinger JM. Synergistic Binding of the Halide and Cationic Prime Substrate of l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States. Biochemistry. PMID 37542461 DOI: 10.1021/acs.biochem.3c00248  0.845
2023 Slater JW, Neugebauer ME, McBride MJ, Sil D, Lin CY, Katch BJ, Boal AK, Chang MCY, Silakov A, Krebs C, Bollinger JM. Synergistic Binding of the Halide and Cationic Prime Substrate of the l-Lysine 4-Chlorinase, BesD, in Both Ferrous and Ferryl States. Biorxiv : the Preprint Server For Biology. PMID 37205437 DOI: 10.1101/2023.05.02.539147  0.842
2023 McBride MJ, Pope SR, Nair MA, Sil D, Salas-Solá XE, Krebs C, Martin Bollinger J, Boal AK. Methods for Biophysical Characterization of SznF, a Member of the Heme-Oxygenase-Like Diiron Oxidase/Oxygenase Superfamily. Methods in Molecular Biology (Clifton, N.J.). 2648: 123-154. PMID 37039989 DOI: 10.1007/978-1-0716-3080-8_9  0.728
2023 Manesis AC, Slater JW, Cantave K, Martin Bollinger J, Krebs C, Rosenzweig AC. Capturing a -Fe(IV) State in OB3b MbnH. Biochemistry. 62: 1082-1092. PMID 36812111 DOI: 10.1021/acs.biochem.3c00021  0.854
2022 Lin CY, Muñoz AL, Laremore TN, Silakov A, Krebs C, Boal AK, Bollinger JM. Use of Noncanonical Tyrosine Analogues to Probe Control of Radical Intermediates during Endoperoxide Installation by Verruculogen Synthase (FtmOx1). Acs Catalysis. 12: 6968-6979. PMID 37744570 DOI: 10.1021/acscatal.2c01037  0.74
2022 Warui DM, Sil D, Lee KH, Neti SS, Esakova OA, Knox HL, Krebs C, Booker SJ. In Vitro Demonstration of Human Lipoyl Synthase Catalytic Activity in the Presence of NFU1. Acs Bio & Med Chem Au. 2: 456-468. PMID 36281303 DOI: 10.1021/acsbiomedchemau.2c00020  0.73
2022 Neti SS, Sil D, Warui DM, Esakova OA, Solinski AE, Serrano DA, Krebs C, Booker SJ. Characterization of LipS1 and LipS2 from : Proteins Annotated as Biotin Synthases, which Together Catalyze Formation of the Lipoyl Cofactor. Acs Bio & Med Chem Au. 2: 509-520. PMID 36281299 DOI: 10.1021/acsbiomedchemau.2c00018  0.739
2022 Dong HT, Camarena S, Sil D, Lengel MO, Zhao J, Hu MY, Alp EE, Krebs C, Lehnert N. What Is the Right Level of Activation of a High-Spin {FeNO} Complex to Enable Direct N-N Coupling? Mechanistic Insight into Flavodiiron NO Reductases. Journal of the American Chemical Society. 144: 16395-16409. PMID 36040133 DOI: 10.1021/jacs.2c04292  0.712
2022 Panth N, Wenger ES, Krebs C, Bollinger JM, Grossman RB. Synthesis of 6,6- and 7,7-difluoro-1-acetamidopyrrolizidines and their oxidation catalyzed by the nonheme Fe oxygenase LolO. Chembiochem : a European Journal of Chemical Biology. PMID 35482316 DOI: 10.1002/cbic.202200081  0.759
2022 McBride MJ, Nair MA, Sil D, Slater JW, Neugebauer ME, Chang MCY, Boal AK, Krebs C, Bollinger JM. Substrate-Triggered μ-Peroxodiiron(III) Intermediate in the 4-Chloro-l-Lysine-Fragmenting Heme-Oxygenase-like Diiron Oxidase (HDO) BesC: Substrate Dissociation from, and C4 Targeting by, the Intermediate. Biochemistry. PMID 35380785 DOI: 10.1021/acs.biochem.1c00774  0.823
2022 Park YJ, Jodts RJ, Slater JW, Reyes RM, Winton VJ, Montaser RA, Thomas PM, Dowdle WB, Ruiz A, Kelleher NL, Bollinger JM, Krebs C, Hoffman BM, Rosenzweig AC. A mixed-valent Fe(II)Fe(III) species converts cysteine to an oxazolone/thioamide pair in methanobactin biosynthesis. Proceedings of the National Academy of Sciences of the United States of America. 119: e2123566119. PMID 35320042 DOI: 10.1073/pnas.2123566119  0.857
2022 Dong HT, Zong Y, Bracken AJ, Lengel MO, Kampf JW, Sil D, Krebs C, Lehnert N. Synthesis and characterization of a model complex for flavodiiron NO reductases that stabilizes a diiron mononitrosyl complex. Journal of Inorganic Biochemistry. 229: 111723. PMID 35074551 DOI: 10.1016/j.jinorgbio.2022.111723  0.736
2021 Esakova OA, Grove TL, Yennawar NH, Arcinas AJ, Wang B, Krebs C, Almo SC, Booker SJ. Structural basis for tRNA methylthiolation by the radical SAM enzyme MiaB. Nature. PMID 34526715 DOI: 10.1038/s41586-021-03904-6  0.346
2021 Copeland R, Zhou S, Schaperdoth I, Shoda TK, Bollinger JM, Krebs C. Hybrid radical-polar pathway for excision of ethylene from 2-oxoglutarate by an iron oxygenase. Science (New York, N.Y.). PMID 34385355 DOI: 10.1126/science.abj4290  0.751
2021 Maio N, Lafont BAP, Sil D, Li Y, Bollinger JM, Krebs C, Pierson TC, Linehan WM, Rouault TA. Fe-S cofactors in the SARS-CoV-2 RNA-dependent RNA polymerase are potential antiviral targets. Science (New York, N.Y.). PMID 34083449 DOI: 10.1126/science.abi5224  0.791
2021 Copeland RA, Davis KM, Shoda TKC, Blaesi EJ, Boal AK, Krebs C, Bollinger JM. An Iron(IV)-Oxo Intermediate Initiating l-Arginine Oxidation but Not Ethylene Production by the 2-Oxoglutarate-Dependent Oxygenase, Ethylene-Forming Enzyme. Journal of the American Chemical Society. PMID 33522811 DOI: 10.1021/jacs.0c10923  0.773
2020 Liu G, Sil D, Maio N, Tong WH, Bollinger JM, Krebs C, Rouault TA. Heme biosynthesis depends on previously unrecognized acquisition of iron-sulfur cofactors in human amino-levulinic acid dehydratase. Nature Communications. 11: 6310. PMID 33298951 DOI: 10.1038/s41467-020-20145-9  0.831
2020 Srnec M, Iyer SR, Dassama LMK, Park K, Wong SD, Sutherlin KD, Yoda Y, Kobayashi Y, Kurokuzu M, Saito M, Seto M, Krebs C, Bollinger JM, Solomon EI. Nuclear Resonance Vibrational Spectroscopic Definition of the Facial Triad Fe═O Intermediate in Taurine Dioxygenase: Evaluation of Structural Contributions to Hydrogen Atom Abstraction. Journal of the American Chemical Society. PMID 33103886 DOI: 10.1021/jacs.0c08903  0.723
2020 McBride M, Sil D, Ng TL, Crooke AM, Kenney GE, Tysoe CR, Zhang B, Balskus EP, Boal AK, Krebs C, Bollinger JM. A peroxodiiron(III) intermediate mediating both -hydroxylation steps in biosynthesis of the -nitrosourea pharmacophore of streptozotocin by SznF. Journal of the American Chemical Society. PMID 32511919 DOI: 10.1021/Jacs.0C03431  0.851
2020 Zhang B, Arcinas AJ, Radle MI, Silakov A, Booker SJ, Krebs C. The First Step in Catalysis of the Radical S-Adenosylmethionine Methylthiotransferase MiaB Yields an Intermediate with a [3Fe-4S]0-like Auxiliary Cluster. Journal of the American Chemical Society. PMID 31899624 DOI: 10.1021/Jacs.9B11093  0.458
2019 Zhou S, Pan J, Davis KM, Schaperdoth I, Wang B, Boal AK, Krebs C, Bollinger JM. Steric enforcement of cis-epoxide formation in the radical C-O-coupling reaction by which (S)-2-hydroxypropylphosphonate epoxidase (HppE) produces Fosfomycin. Journal of the American Chemical Society. PMID 31769979 DOI: 10.1021/Jacs.9B10974  0.718
2019 Cutsail GE, Blaesi EJ, Pollock CJ, Bollinger JM, Krebs C, DeBeer S. High-resolution iron X-ray absorption spectroscopic and computational studies of non-heme diiron peroxo intermediates. Journal of Inorganic Biochemistry. 203: 110877. PMID 31710865 DOI: 10.1016/J.Jinorgbio.2019.110877  0.831
2019 Dong HT, Speelman AL, Kozemchak CE, Sil D, Krebs C, Lehnert N. The Fe₂(NO)₂ Diamond Core: A Unique Structural Motif in Non-Heme Iron-NO Chemistry. Angewandte Chemie (International Ed. in English). PMID 31550416 DOI: 10.1002/Anie.201911968  0.761
2019 Davis KM, Altmyer M, Martinie RJ, Schaperdoth I, Krebs C, Bollinger JM, Boal AK. Structure of a ferryl mimic in the archetypal iron(II)- and 2-(oxo)-glutarate-dependent dioxygenase, TauD. Biochemistry. PMID 31503454 DOI: 10.1021/Acs.Biochem.9B00598  0.853
2019 Zhang B, Rajakovich LJ, Van Cura D, Blaesi EJ, Mitchell AJ, Tysoe CR, Zhu X, Streit BR, Rui Z, Zhang W, Boal AK, Krebs C, Bollinger JM. Substrate-triggered Formation of a Peroxo-Fe(III/III) Intermediate during Fatty Acid Decarboxylation by UndA. Journal of the American Chemical Society. PMID 31487162 DOI: 10.1021/Jacs.9B06093  0.867
2019 Pan J, Wenger ES, Matthews ML, Pollock CJ, Bhardwaj M, Kim AJ, Allen BD, Grossman RB, Krebs C, Bollinger JM. Evidence for Modulation of Oxygen-Rebound Rate in Control of Outcome by Iron(II)- and 2-Oxoglutarate-Dependent Oxygenases. Journal of the American Chemical Society. PMID 31475820 DOI: 10.1021/Jacs.9B06689  0.847
2019 Gumkowski JD, Martinie RJ, Corrigan P, Pan J, Bauerle MR, Almarei M, Booker SJ, Silakov A, Krebs C, Boal AK. Analysis of RNA methylation by phylogenetically diverse Cfr radical SAM enzymes reveals an iron-binding accessory domain in a clostridial enzyme. Biochemistry. PMID 31246421 DOI: 10.1021/Acs.Biochem.9B00197  0.795
2019 Chekan JR, Ongpipattanakul C, Wright TR, Zhang B, Bollinger JM, Rajakovich LJ, Krebs C, Cicchillo RM, Nair SK. Molecular basis for enantioselective herbicide degradation imparted by aryloxyalkanoate dioxygenases in transgenic plants. Proceedings of the National Academy of Sciences of the United States of America. PMID 31209034 DOI: 10.1073/Pnas.1900711116  0.829
2019 Dunham NP, Del Río Pantoja JM, Zhang B, Rajakovich LJ, Allen BD, Krebs C, Boal AK, Bollinger JM. Hydrogen Donation but not Abstraction by a Tyrosine (Y68) During Endoperoxide Installation by Verruculogen Synthase (FtmOx1). Journal of the American Chemical Society. PMID 31117657 DOI: 10.2210/Pdb6Oxj/Pdb  0.848
2019 Rajakovich L, Pandelia ME, Mitchell AJ, Chang WC, Zhang B, Boal AK, Krebs C, Bollinger JM. A new microbial pathway for organophosphonate degradation catalyzed by two previously misannotated non-heme-iron oxygenases. Biochemistry. PMID 30789718 DOI: 10.1021/acs.biochem.9b00044  0.829
2019 McQuarters AB, Blaesi EJ, Kampf JW, Alp EE, Zhao J, Hu M, Krebs C, Lehnert N. Synthetic Model Complex of the Key Intermediate in Cytochrome P450 Nitric Oxide Reductase. Inorganic Chemistry. PMID 30623648 DOI: 10.1021/Acs.Inorgchem.8B02947  0.529
2018 Dunham NP, Mitchell AJ, Del Río Pantoja JM, Krebs C, Bollinger JM, Boal AK. α-Amine Desaturation of d-Arginine by the Iron(II)- and 2-(Oxo)glutarate-Dependent l-Arginine 3-Hydroxylase, VioC. Biochemistry. PMID 30403469 DOI: 10.1021/Acs.Biochem.8B00901  0.802
2018 Blaesi EJ, Palowitch GM, Hu K, Kim AJ, Rose HR, Alapati R, Lougee MG, Kim HJ, Taguchi AT, Tan KO, Laremore TN, Griffin RG, Krebs C, Matthews ML, Silakov A, et al. Metal-free class Ie ribonucleotide reductase from pathogens initiates catalysis with a tyrosine-derived dihydroxyphenylalanine radical. Proceedings of the National Academy of Sciences of the United States of America. PMID 30224458 DOI: 10.1073/Pnas.1811993115  0.803
2018 Dong H, White CJ, Zhang B, Krebs C, Lehnert N. Non-Heme Diiron Model Complexes Can Mediate Direct NO Reduction: Mechanistic Insight Into Flavodiiron NO Reductases. Journal of the American Chemical Society. PMID 30220202 DOI: 10.1021/Jacs.8B08567  0.408
2018 Grell TAJ, Kincannon WM, Bruender NA, Blaesi EJ, Krebs C, Bandarian V, Drennan CL. Structural and spectroscopic analyses of the sporulation killing factor biosynthetic enzyme SkfB, a bacterial AdoMet radical sactisynthase. The Journal of Biological Chemistry. PMID 30217813 DOI: 10.1074/Jbc.Ra118.005369  0.463
2018 Speelman AL, White CJ, Zhang B, Alp EE, Zhao J, Hu M, Krebs C, Penner-Hahn J, Lehnert N. Non-Heme High-Spin {FeNO} Complexes: One Ligand Platform Can Do It All. Journal of the American Chemical Society. PMID 30107126 DOI: 10.1021/Jacs.8B06095  0.523
2018 Martinie RJ, Blaesi EJ, Bollinger JM, Krebs C, Finkelstein KD, Pollock C. Two-Color Valence-to-Core X-ray Emission Spectroscopy Tracks Cofactor Protonation State in a Class I Ribonucleotide Reductase. Angewandte Chemie (International Ed. in English). PMID 30075052 DOI: 10.1002/Anie.201807366  0.811
2018 Wang B, Blaszczyk AJ, Knox H, Zhou S, Blaesi EJ, Krebs C, Wang R, Booker SJ. Stereochemical and Mechanistic Investigation of the Reaction Catalyzed by Fom3 from Streptomyces fradiae, a Cobalamin-Dependent Radical S-Adenosylmethionine Methylase. Biochemistry. PMID 30036047 DOI: 10.1021/Acs.Biochem.8B00693  0.43
2018 Prakash D, Walters KA, Martinie RJ, McCarver AC, Kumar AK, Lessner DJ, Krebs C, Golbeck JH, Ferry JG. Towards a mechanistic and physiological understanding of a ferredoxin disulfide reductase from the domains and . The Journal of Biological Chemistry. PMID 29720404 DOI: 10.1074/Jbc.Ra118.002473  0.824
2018 Dunham NP, Chang WC, Mitchell AJ, Martinie RJ, Zhang B, Bergman JA, Rajakovich LJ, Wang B, Silakov A, Krebs C, Boal AK, Bollinger JM. Two Distinct Mechanisms for C-C Desaturation by Iron(II)- and 2-(Oxo)glutarate-Dependent Oxygenases: Importance of α-Heteroatom Assistance. Journal of the American Chemical Society. PMID 29708749 DOI: 10.1021/Jacs.8B01933  0.846
2018 Rose H, Ghosh M, Maggiolo A, Pollock CJ, Blaesi EJ, Hajj V, Wei Y, Rajakovich LJ, Chang WC, Han Y, Hajj M, Krebs C, Silakov A, Pandelia ME, Bollinger JM, et al. Structural Basis for Superoxide Activation of Flavobacterium johnsoniae Class I Ribonucleotide Reductase and for Radical Initiation by its Dimanganese Cofactor. Biochemistry. PMID 29609464 DOI: 10.1021/Acs.Biochem.8B00247  0.809
2018 Kenney GE, Dassama LMK, Pandelia ME, Gizzi AS, Martinie RJ, Gao P, DeHart CJ, Schachner LF, Skinner OS, Ro SY, Zhu X, Sadek M, Thomas PM, Almo SC, Bollinger JM, ... Krebs C, et al. The biosynthesis of methanobactin. Science (New York, N.Y.). 359: 1411-1416. PMID 29567715 DOI: 10.1126/Science.Aap9437  0.798
2018 Pan J, Bhardwaj M, Zhang B, Chang WC, Schardl CL, Krebs C, Grossman RB, Bollinger JM. Installation of the ether bridge of lolines by the iron- and 2-oxoglutarate-dependent oxygenase, LolO: regio- and stereochemistry of sequential hydroxylation and oxacyclization reactions. Biochemistry. PMID 29537853 DOI: 10.1021/Acs.Biochem.8B00157  0.784
2017 Martinie RJ, Pollock CJ, Matthews ML, Bollinger JM, Krebs C, Silakov A. Vanadyl as a Stable Structural Mimic of Reactive Ferryl Intermediates in Mononuclear Nonheme-Iron Enzymes. Inorganic Chemistry. 56: 13382-13389. PMID 28960972 DOI: 10.1021/Acs.Inorgchem.7B02113  0.865
2017 Mitchell AJ, Dunham NP, Martinie RJ, Bergman JA, Pollock CJ, Hu K, Allen BD, Chang WC, Silakov A, Bollinger JM, Krebs C, Boal AK. Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase. Journal of the American Chemical Society. 139: 13830-13836. PMID 28823155 DOI: 10.1021/Jacs.7B07374  0.856
2017 Park K, Li N, Kwak Y, Srnec M, Bell CB, Liu LV, Wong SD, Yoda Y, Kitao S, Seto M, Hu M, Zhao J, Krebs C, Bollinger JM, Solomon EI. Peroxide Activation for Electrophilic Reactivity by the Binuclear Non-heme Iron Enzyme AurF. Journal of the American Chemical Society. 139: 7062-7070. PMID 28457126 DOI: 10.1021/Jacs.7B02997  0.77
2017 Tanner AW, Carabetta VJ, Martinie RJ, Mashruwala AA, Boyd JM, Krebs C, Dubnau D. The RicAFT (YmcA-YlbF-YaaT) complex carries two [4Fe-4S](2+) clusters and may respond to redox changes. Molecular Microbiology. PMID 28295778 DOI: 10.1111/Mmi.13667  0.802
2017 Fuller FD, Gul S, Chatterjee R, Burgie ES, Young ID, Lebrette H, Srinivas V, Brewster AS, Michels-Clark T, Clinger JA, Andi B, Ibrahim M, Pastor E, de Lichtenberg C, Hussein R, ... ... Krebs C, et al. Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers. Nature Methods. 14: 443-449. PMID 28250468 DOI: 10.1038/Nmeth.4195  0.78
2017 Peck SC, Wang C, Dassama LM, Zhang B, Guo Y, Rajakovich LJ, Bollinger JM, Krebs C, van der Donk WA. O-H Activation by an Unexpected Ferryl Intermediate during Catalysis by 2-Hydroxyethylphosphonate Dioxygenase. Journal of the American Chemical Society. 139: 2045-2052. PMID 28092705 DOI: 10.1021/Jacs.6B12147  0.817
2017 Martinie RJ, Blaesi EJ, Krebs C, Bollinger JM, Silakov A, Pollock CJ. Evidence for a Di-μ-oxo Diamond Core in the Mn(IV)/Fe(IV) Activation Intermediate of Ribonucleotide Reductase from Chlamydia trachomatis. Journal of the American Chemical Society. 139: 1950-1957. PMID 28075562 DOI: 10.1021/Jacs.6B11563  0.866
2016 Sahu S, Zhang B, Pollock CJ, Dürr M, Davies CG, Confer AM, Ivanović-Burmazović I, Siegler MA, Jameson GN, Krebs C, Goldberg DP. Aromatic C-F Hydroxylation by Nonheme Iron(IV)-Oxo Complexes: Structural, Spectroscopic, and Mechanistic Investigations. Journal of the American Chemical Society. PMID 27656776 DOI: 10.1021/Jacs.6B03346  0.781
2016 Dong M, Horitani M, Dzikovski B, Pandelia ME, Krebs C, Freed JH, Hoffman BM, Lin H. An organometallic complex formed by an unconventional radical SAM enzyme. Journal of the American Chemical Society. PMID 27465315 DOI: 10.1021/Jacs.6B04155  0.54
2016 Speelman AL, Zhang B, Silakov A, Skodje KM, Alp EE, Zhao J, Hu MY, Kim E, Krebs C, Lehnert N. Unusual Synthetic Pathway for an {Fe(NO)2}(9) Dinitrosyl Iron Complex (DNIC) and Insight into DNIC Electronic Structure via Nuclear Resonance Vibrational Spectroscopy. Inorganic Chemistry. PMID 27203448 DOI: 10.1021/Acs.Inorgchem.6B00510  0.552
2016 Tamanaha E, Zhang B, Guo Y, Chang WC, Barr EW, Xing G, St Clair J, Ye S, Neese F, Bollinger JM, Krebs C. Spectroscopic Evidence for the Two C-H-Cleaving Intermediates of Aspergillus nidulans Isopenicillin N Synthase. Journal of the American Chemical Society. 138: 8862-74. PMID 27193226 DOI: 10.1021/Jacs.6B04065  0.759
2016 Speelman AL, Zhang B, Krebs C, Lehnert N. Structural and Spectroscopic Characterization of a High-Spin {FeNO}(6) Complex with an Iron(IV)-NO(-) Electronic Structure. Angewandte Chemie (International Ed. in English). PMID 27101151 DOI: 10.1002/Anie.201601742  0.397
2016 Srnec M, Wong SD, Matthews ML, Krebs C, Bollinger JM, Solomon EI. Electronic Structure of the Ferryl Intermediate in the α-Ketoglutarate Dependent Non-Heme Iron Halogenase SyrB2: Contributions to H Atom Abstraction Reactivity. Journal of the American Chemical Society. 138: 5110-22. PMID 27021969 DOI: 10.1021/Jacs.6B01151  0.839
2016 Blaszczyk AJ, Silakov A, Zhang B, Maiocco SJ, Lanz ND, Kelly WL, Elliott SJ, Krebs C, Booker SJ. Spectroscopic and Electrochemical Characterization of the Iron-Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase. Journal of the American Chemical Society. PMID 26841310 DOI: 10.1021/Jacs.5B12592  0.556
2016 Lanz ND, Lee KH, Horstmann AK, Pandelia ME, Cicchillo RM, Krebs C, Booker SJ. Characterization of Lipoyl Synthase from Mycobacterium tuberculosis. Biochemistry. PMID 26841001 DOI: 10.1021/Acs.Biochem.5B01216  0.415
2015 Nakashige TG, Zhang B, Krebs C, Nolan EM. Human calprotectin is an iron-sequestering host-defense protein. Nature Chemical Biology. 11: 765-71. PMID 26302479 DOI: 10.1038/Nchembio.1891  0.497
2015 Rajakovich LJ, Nørgaard H, Warui DM, Chang WC, Li N, Booker SJ, Krebs C, Bollinger JM, Pandelia ME. Rapid Reduction of the Diferric-Peroxyhemiacetal Intermediate in Aldehyde-Deformylating Oxygenase by a Cyanobacterial Ferredoxin: Evidence for a Free-Radical Mechanism. Journal of the American Chemical Society. 137: 11695-709. PMID 26284355 DOI: 10.1021/Jacs.5B06345  0.832
2015 Livada J, Martinie RJ, Dassama LM, Krebs C, Bollinger JM, Silakov A. Direct Measurement of the Radical Translocation Distance in the Class I Ribonucleotide Reductase from Chlamydia trachomatis. The Journal of Physical Chemistry. B. 119: 13777-84. PMID 26087051 DOI: 10.1021/Acs.Jpcb.5B04067  0.83
2015 Martinie RJ, Livada J, Chang WC, Green MT, Krebs C, Bollinger JM, Silakov A. Experimental Correlation of Substrate Position with Reaction Outcome in the Aliphatic Halogenase, SyrB2. Journal of the American Chemical Society. 137: 6912-9. PMID 25965587 DOI: 10.1021/Jacs.5B03370  0.848
2015 Pandelia ME, Lanz ND, Booker SJ, Krebs C. Mössbauer spectroscopy of Fe/S proteins. Biochimica Et Biophysica Acta. 1853: 1395-1405. PMID 25498248 DOI: 10.1016/J.Bbamcr.2014.12.005  0.511
2015 Warui DM, Pandelia ME, Rajakovich LJ, Krebs C, Bollinger JM, Booker SJ. Efficient delivery of long-chain fatty aldehydes from the Nostoc punctiforme acyl-acyl carrier protein reductase to its cognate aldehyde-deformylating oxygenase. Biochemistry. 54: 1006-15. PMID 25496470 DOI: 10.1021/Bi500847U  0.795
2015 Bollinger JM, Chang WC, Matthews ML, Martinie RJ, Boal AK, Krebs C. Mechanisms of 2-oxoglutarate-dependent oxygenases: The hydroxylation paradigm and beyond Rsc Metallobiology. 2015: 95-122. DOI: 10.1039/9781782621959-00095  0.773
2014 Lanz ND, Pandelia ME, Kakar ES, Lee KH, Krebs C, Booker SJ. Evidence for a catalytically and kinetically competent enzyme-substrate cross-linked intermediate in catalysis by lipoyl synthase. Biochemistry. 53: 4557-72. PMID 24901788 DOI: 10.1021/Bi500432R  0.488
2014 Ludwig M, Pandelia ME, Chew CY, Zhang B, Golbeck JH, Krebs C, Bryant DA. ChlR protein of Synechococcus sp. PCC 7002 is a transcription activator that uses an oxygen-sensitive [4Fe-4S] cluster to control genes involved in pigment biosynthesis. The Journal of Biological Chemistry. 289: 16624-39. PMID 24782315 DOI: 10.1074/Jbc.M114.561233  0.429
2014 Chang WC, Guo Y, Wang C, Butch SE, Rosenzweig AC, Boal AK, Krebs C, Bollinger JM. Mechanism of the C5 stereoinversion reaction in the biosynthesis of carbapenem antibiotics. Science (New York, N.Y.). 343: 1140-4. PMID 24604200 DOI: 10.1126/Science.1248000  0.853
2014 Matthews ML, Chang WC, Layne AP, Miles LA, Krebs C, Bollinger JM. Direct nitration and azidation of aliphatic carbons by an iron-dependent halogenase. Nature Chemical Biology. 10: 209-15. PMID 24463698 DOI: 10.1038/Nchembio.1438  0.848
2013 Krebs C, Dassama LM, Matthews ML, Jiang W, Price JC, Korboukh V, Li N, Bollinger JM. Novel Approaches for the Accumulation of Oxygenated Intermediates to Multi-Millimolar Concentrations. Coordination Chemistry Reviews. 257. PMID 24368870 DOI: 10.1016/J.Ccr.2012.06.020  0.802
2013 Wörsdörfer B, Lingaraju M, Yennawar NH, Boal AK, Krebs C, Bollinger JM, Pandelia ME. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proceedings of the National Academy of Sciences of the United States of America. 110: 18874-9. PMID 24198335 DOI: 10.1073/Pnas.1315927110  0.801
2013 Kwak Y, Jiang W, Dassama LM, Park K, Bell CB, Liu LV, Wong SD, Saito M, Kobayashi Y, Kitao S, Seto M, Yoda Y, Alp EE, Zhao J, Bollinger JM, ... Krebs C, et al. Geometric and electronic structure of the Mn(IV)Fe(III) cofactor in class Ic ribonucleotide reductase: correlation to the class Ia binuclear non-heme iron enzyme. Journal of the American Chemical Society. 135: 17573-84. PMID 24131208 DOI: 10.1021/Ja409510D  0.853
2013 Wang C, Chang WC, Guo Y, Huang H, Peck SC, Pandelia ME, Lin GM, Liu HW, Krebs C, Bollinger JM. Evidence that the fosfomycin-producing epoxidase, HppE, is a non-heme-iron peroxidase. Science (New York, N.Y.). 342: 991-5. PMID 24114783 DOI: 10.1126/Science.1240373  0.781
2013 Dassama LM, Silakov A, Krest CM, Calixto JC, Krebs C, Bollinger JM, Green MT. A 2.8 Å Fe-Fe separation in the Fe2(III/IV) intermediate, X, from Escherichia coli ribonucleotide reductase. Journal of the American Chemical Society. 135: 16758-61. PMID 24094084 DOI: 10.1021/Ja407438P  0.861
2013 Snyder RA, Bell CB, Diao Y, Krebs C, Bollinger JM, Solomon EI. Circular dichroism, magnetic circular dichroism, and variable temperature variable field magnetic circular dichroism studies of biferrous and mixed-valent myo-inositol oxygenase: insights into substrate activation of O2 reactivity. Journal of the American Chemical Society. 135: 15851-63. PMID 24066857 DOI: 10.1021/Ja406635K  0.792
2013 Bill E, Krebs C, Winter M, Gerdan M, Trautwein AX, Flörke U, Haupt HJ, Chaudhuri P. A Triangular Iron(III) Complex Potentially Relevant to Iron(III)-Binding Sites in Ferreascidin. Chemistry (Weinheim An Der Bergstrasse, Germany). 3: 193-201. PMID 24022947 DOI: 10.1002/Chem.19970030205  0.506
2013 Anton BP, Chang YC, Brown P, Choi HP, Faller LL, Guleria J, Hu Z, Klitgord N, Levy-Moonshine A, Maksad A, Mazumdar V, McGettrick M, Osmani L, Pokrzywa R, Rachlin J, ... ... Krebs C, et al. The COMBREX project: design, methodology, and initial results. Plos Biology. 11: e1001638. PMID 24013487 DOI: 10.1371/Journal.Pbio.1001638  0.638
2013 Pandelia ME, Li N, Nørgaard H, Warui DM, Rajakovich LJ, Chang WC, Booker SJ, Krebs C, Bollinger JM. Substrate-triggered addition of dioxygen to the diferrous cofactor of aldehyde-deformylating oxygenase to form a diferric-peroxide intermediate. Journal of the American Chemical Society. 135: 15801-12. PMID 23987523 DOI: 10.1021/Ja405047B  0.862
2013 Dassama LM, Krebs C, Bollinger JM, Rosenzweig AC, Boal AK. Structural basis for assembly of the Mn(IV)/Fe(III) cofactor in the class Ic ribonucleotide reductase from Chlamydia trachomatis. Biochemistry. 52: 6424-36. PMID 23924396 DOI: 10.1021/Bi400819X  0.844
2013 Wong SD, Srnec M, Matthews ML, Liu LV, Kwak Y, Park K, Bell CB, Alp EE, Zhao J, Yoda Y, Kitao S, Seto M, Krebs C, Bollinger JM, Solomon EI. Elucidation of the Fe(IV)=O intermediate in the catalytic cycle of the halogenase SyrB2. Nature. 499: 320-3. PMID 23868262 DOI: 10.1038/Nature12304  0.85
2013 Wörsdörfer B, Conner DA, Yokoyama K, Livada J, Seyedsayamdost M, Jiang W, Silakov A, Stubbe J, Bollinger JM, Krebs C. Function of the diiron cluster of Escherichia coli class Ia ribonucleotide reductase in proton-coupled electron transfer. Journal of the American Chemical Society. 135: 8585-93. PMID 23676140 DOI: 10.1021/Ja401342S  0.835
2013 Grove TL, Ahlum JH, Qin RM, Lanz ND, Radle MI, Krebs C, Booker SJ. Further characterization of Cys-type and Ser-type anaerobic sulfatase maturating enzymes suggests a commonality in the mechanism of catalysis. Biochemistry. 52: 2874-87. PMID 23477283 DOI: 10.1021/Bi400136U  0.5
2013 McCarty RM, Krebs C, Bandarian V. Spectroscopic, steady-state kinetic, and mechanistic characterization of the radical SAM enzyme QueE, which catalyzes a complex cyclization reaction in the biosynthesis of 7-deazapurines. Biochemistry. 52: 188-98. PMID 23194065 DOI: 10.1021/Bi301156W  0.454
2012 Dassama LM, Jiang W, Varano PT, Pandelia ME, Conner DA, Xie J, Bollinger JM, Krebs C. Radical-translocation intermediates and hurdling of pathway defects in "super-oxidized" (Mn(IV)/Fe(IV)) Chlamydia trachomatis ribonucleotide reductase. Journal of the American Chemical Society. 134: 20498-506. PMID 23157728 DOI: 10.1021/Ja309468S  0.857
2012 Lanz ND, Grove TL, Gogonea CB, Lee KH, Krebs C, Booker SJ. RlmN and AtsB as models for the overproduction and characterization of radical SAM proteins. Methods in Enzymology. 516: 125-52. PMID 23034227 DOI: 10.1016/B978-0-12-394291-3.00030-7  0.48
2012 Li N, Chang WC, Warui DM, Booker SJ, Krebs C, Bollinger JM. Evidence for only oxygenative cleavage of aldehydes to alk(a/e)nes and formate by cyanobacterial aldehyde decarbonylases. Biochemistry. 51: 7908-16. PMID 22947199 DOI: 10.1021/Bi300912N  0.723
2012 Ye S, Riplinger C, Hansen A, Krebs C, Bollinger JM, Neese F. Electronic structure analysis of the oxygen-activation mechanism by Fe(II)- and α-ketoglutarate (αKG)-dependent dioxygenases. Chemistry (Weinheim An Der Bergstrasse, Germany). 18: 6555-67. PMID 22511515 DOI: 10.1002/Chem.201102829  0.771
2012 Dassama LM, Yosca TH, Conner DA, Lee MH, Blanc B, Streit BR, Green MT, DuBois JL, Krebs C, Bollinger JM. O(2)-evolving chlorite dismutase as a tool for studying O(2)-utilizing enzymes. Biochemistry. 51: 1607-16. PMID 22304240 DOI: 10.1021/Bi201906X  0.802
2012 Dassama LM, Boal AK, Krebs C, Rosenzweig AC, Bollinger JM. Evidence that the β subunit of Chlamydia trachomatis ribonucleotide reductase is active with the manganese ion of its manganese(IV)/iron(III) cofactor in site 1. Journal of the American Chemical Society. 134: 2520-3. PMID 22242660 DOI: 10.1021/Ja211314P  0.849
2012 Bhave DP, Hong JA, Keller RL, Krebs C, Carroll KS. Iron-sulfur cluster engineering provides insight into the evolution of substrate specificity among sulfonucleotide reductases. Acs Chemical Biology. 7: 306-15. PMID 22023093 DOI: 10.1021/Cb200261N  0.447
2011 Grove TL, Radle MI, Krebs C, Booker SJ. Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation. Journal of the American Chemical Society. 133: 19586-9. PMID 21916495 DOI: 10.1021/Ja207327V  0.509
2011 Li N, Nørgaard H, Warui DM, Booker SJ, Krebs C, Bollinger JM. Conversion of fatty aldehydes to alka(e)nes and formate by a cyanobacterial aldehyde decarbonylase: cryptic redox by an unusual dimetal oxygenase. Journal of the American Chemical Society. 133: 6158-61. PMID 21462983 DOI: 10.1021/Ja2013517  0.759
2011 Krebs C, Bollinger JM, Booker SJ. Cyanobacterial alkane biosynthesis further expands the catalytic repertoire of the ferritin-like 'di-iron-carboxylate' proteins. Current Opinion in Chemical Biology. 15: 291-303. PMID 21440485 DOI: 10.1016/J.Cbpa.2011.02.019  0.777
2011 Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ. A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. Science (New York, N.Y.). 332: 604-7. PMID 21415317 DOI: 10.1126/Science.1200877  0.332
2011 Warui DM, Li N, Nørgaard H, Krebs C, Bollinger JM, Booker SJ. Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a cyanobacterial aldehyde decarbonylase. Journal of the American Chemical Society. 133: 3316-9. PMID 21341652 DOI: 10.1021/Ja111607X  0.729
2011 Panay AJ, Lee M, Krebs C, Bollinger JM, Fitzpatrick PF. Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase. Biochemistry. 50: 1928-33. PMID 21261288 DOI: 10.1021/Bi1019868  0.806
2011 Bhave DP, Hong JA, Lee M, Jiang W, Krebs C, Carroll KS. Spectroscopic studies on the [4Fe-4S] cluster in adenosine 5'-phosphosulfate reductase from Mycobacterium tuberculosis. The Journal of Biological Chemistry. 286: 1216-26. PMID 21075841 DOI: 10.1074/Jbc.M110.193722  0.488
2011 Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H. Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme (Nature (2010) 465 (891-896)) Nature. 473: 544. DOI: 10.1038/Nature10087  0.422
2010 van der Donk WA, Krebs C, Bollinger JM. Substrate activation by iron superoxo intermediates. Current Opinion in Structural Biology. 20: 673-83. PMID 20951572 DOI: 10.1016/J.Sbi.2010.08.005  0.813
2010 Flashman E, Hoffart LM, Hamed RB, Bollinger JM, Krebs C, Schofield CJ. Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen. The Febs Journal. 277: 4089-99. PMID 20840591 DOI: 10.1111/J.1742-4658.2010.07804.X  0.709
2010 Song WJ, McCormick MS, Behan RK, Sazinsky MH, Jiang W, Lin J, Krebs C, Lippard SJ. Active site threonine facilitates proton transfer during dioxygen activation at the diiron center of toluene/o-xylene monooxygenase hydroxylase. Journal of the American Chemical Society. 132: 13582-5. PMID 20839885 DOI: 10.1021/Ja1063795  0.373
2010 Li N, Korboukh VK, Krebs C, Bollinger JM. Four-electron oxidation of p-hydroxylaminobenzoate to p-nitrobenzoate by a peroxodiferric complex in AurF from Streptomyces thioluteus. Proceedings of the National Academy of Sciences of the United States of America. 107: 15722-7. PMID 20798054 DOI: 10.1073/Pnas.1002785107  0.751
2010 Zhang Y, Zhu X, Torelli AT, Lee M, Dzikovski B, Koralewski RM, Wang E, Freed J, Krebs C, Ealick SE, Lin H. Diphthamide biosynthesis requires an organic radical generated by an iron-sulphur enzyme. Nature. 465: 891-6. PMID 20559380 DOI: 10.1038/Nature09138  0.526
2010 Jiang W, Xie J, Varano PT, Krebs C, Bollinger JM. Two distinct mechanisms of inactivation of the class Ic ribonucleotide reductase from Chlamydia trachomatis by hydroxyurea: implications for the protein gating of intersubunit electron transfer. Biochemistry. 49: 5340-9. PMID 20462199 DOI: 10.1021/Bi100037B  0.787
2010 Grove TL, Ahlum JH, Sharma P, Krebs C, Booker SJ. A consensus mechanism for Radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters. Biochemistry. 49: 3783-5. PMID 20377206 DOI: 10.1021/Bi9022126  0.474
2010 Ye S, Price JC, Barr EW, Green MT, Bollinger JM, Krebs C, Neese F. Cryoreduction of the NO-adduct of taurine:alpha-ketoglutarate dioxygenase (TauD) yields an elusive {FeNO}(8) species. Journal of the American Chemical Society. 132: 4739-51. PMID 20218714 DOI: 10.1021/Ja909715G  0.812
2009 Matthews ML, Neumann CS, Miles LA, Grove TL, Booker SJ, Krebs C, Walsh CT, Bollinger JM. Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2. Proceedings of the National Academy of Sciences of the United States of America. 106: 17723-8. PMID 19815524 DOI: 10.1073/Pnas.0909649106  0.83
2009 Lee KH, Saleh L, Anton BP, Madinger CL, Benner JS, Iwig DF, Roberts RJ, Krebs C, Booker SJ. Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily. Biochemistry. 48: 10162-74. PMID 19736993 DOI: 10.1021/Bi900939W  0.488
2009 Korboukh VK, Li N, Barr EW, Bollinger JM, Krebs C. A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus. Journal of the American Chemical Society. 131: 13608-9. PMID 19731912 DOI: 10.1021/Ja9064969  0.789
2009 Matthews ML, Krest CM, Barr EW, Vaillancourt FH, Walsh CT, Green MT, Krebs C, Bollinger JM. Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2. Biochemistry. 48: 4331-43. PMID 19245217 DOI: 10.1021/Bi900109Z  0.823
2009 Krebs C, Bollinger JM. Freeze-quench (57)Fe-Mössbauer spectroscopy: trapping reactive intermediates. Photosynthesis Research. 102: 295-304. PMID 19238577 DOI: 10.1007/S11120-009-9406-6  0.784
2009 Bollinger JM, Diao Y, Matthews ML, Xing G, Krebs C. myo-Inositol oxygenase: a radical new pathway for O(2) and C-H activation at a nonheme diiron cluster. Dalton Transactions (Cambridge, England : 2003). 905-14. PMID 19173070 DOI: 10.1039/B811885J  0.845
2008 Jiang W, Yun D, Saleh L, Bollinger JM, Krebs C. Formation and function of the Manganese(IV)/Iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase. Biochemistry. 47: 13736-44. PMID 19061340 DOI: 10.1021/Bi8017625  0.798
2008 Bollinger JM, Jiang W, Green MT, Krebs C. The manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase: structure, assembly, radical initiation, and evolution. Current Opinion in Structural Biology. 18: 650-7. PMID 19046875 DOI: 10.1016/J.Sbi.2008.11.007  0.773
2008 Chatterjee A, Li Y, Zhang Y, Grove TL, Lee M, Krebs C, Booker SJ, Begley TP, Ealick SE. Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily. Nature Chemical Biology. 4: 758-65. PMID 18953358 DOI: 10.1038/Nchembio.121  0.443
2008 Younker JM, Krest CM, Jiang W, Krebs C, Bollinger JM, Green MT. Structural analysis of the Mn(IV)/Fe(III) cofactor of Chlamydia trachomatis ribonucleotide reductase by extended X-ray absorption fine structure spectroscopy and density functional theory calculations. Journal of the American Chemical Society. 130: 15022-7. PMID 18937466 DOI: 10.1021/Ja804365E  0.778
2008 Saunders AH, Griffiths AE, Lee KH, Cicchillo RM, Tu L, Stromberg JA, Krebs C, Booker SJ. Characterization of quinolinate synthases from Escherichia coli, Mycobacterium tuberculosis, and Pyrococcus horikoshii indicates that [4Fe-4S] clusters are common cofactors throughout this class of enzymes. Biochemistry. 47: 10999-1012. PMID 18803397 DOI: 10.1021/Bi801268F  0.524
2008 Jin Z, Heinnickel M, Krebs C, Shen G, Golbeck JH, Bryant DA. Biogenesis of iron-sulfur clusters in photosystem I: holo-NfuA from the cyanobacterium Synechococcus sp. PCC 7002 rapidly and efficiently transfers [4Fe-4S] clusters to apo-PsaC in vitro. The Journal of Biological Chemistry. 283: 28426-35. PMID 18694929 DOI: 10.1074/Jbc.M803395200  0.482
2008 Jiang W, Saleh L, Barr EW, Xie J, Gardner MM, Krebs C, Bollinger JM. Branched activation- and catalysis-specific pathways for electron relay to the manganese/iron cofactor in ribonucleotide reductase from Chlamydia trachomatis. Biochemistry. 47: 8477-84. PMID 18656954 DOI: 10.1021/Bi800881M  0.768
2008 Li X, Fu R, Lee S, Krebs C, Davidson VL, Liu A. A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical. Proceedings of the National Academy of Sciences of the United States of America. 105: 8597-600. PMID 18562294 DOI: 10.1073/Pnas.0801643105  0.585
2008 Grove TL, Lee KH, St Clair J, Krebs C, Booker SJ. In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters. Biochemistry. 47: 7523-38. PMID 18558715 DOI: 10.1021/Bi8004297  0.535
2008 Jiang W, Xie J, Nørgaard H, Bollinger JM, Krebs C. Rapid and quantitative activation of Chlamydia trachomatis ribonucleotide reductase by hydrogen peroxide. Biochemistry. 47: 4477-83. PMID 18358006 DOI: 10.1021/Bi702085Z  0.796
2008 Hristova D, Wu CH, Jiang W, Krebs C, Stubbe J. Importance of the maintenance pathway in the regulation of the activity of Escherichia coli ribonucleotide reductase. Biochemistry. 47: 3989-99. PMID 18314964 DOI: 10.1021/Bi702408K  0.521
2007 Neidig ML, Brown CD, Light KM, Fujimori DG, Nolan EM, Price JC, Barr EW, Bollinger JM, Krebs C, Walsh CT, Solomon EI. CD and MCD of CytC3 and taurine dioxygenase: role of the facial triad in alpha-KG-dependent oxygenases. Journal of the American Chemical Society. 129: 14224-31. PMID 17967013 DOI: 10.1021/Ja074557R  0.725
2007 Fujimori DG, Barr EW, Matthews ML, Koch GM, Yonce JR, Walsh CT, Bollinger JM, Krebs C, Riggs-Gelasco PJ. Spectroscopic evidence for a high-spin Br-Fe(IV)-oxo intermediate in the alpha-ketoglutarate-dependent halogenase CytC3 from Streptomyces. Journal of the American Chemical Society. 129: 13408-9. PMID 17939667 DOI: 10.1021/Ja076454E  0.841
2007 Wu CH, Jiang W, Krebs C, Stubbe J. YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in Escherichia coli ribonucleotide reductase. Biochemistry. 46: 11577-88. PMID 17880186 DOI: 10.1021/Bi7012454  0.59
2007 Shen G, Balasubramanian R, Wang T, Wu Y, Hoffart LM, Krebs C, Bryant DA, Golbeck JH. SufR coordinates two [4Fe-4S]2+, 1+ clusters and functions as a transcriptional repressor of the sufBCDS operon and an autoregulator of sufR in cyanobacteria. The Journal of Biological Chemistry. 282: 31909-19. PMID 17827500 DOI: 10.1074/Jbc.M705554200  0.441
2007 Krebs C, Matthews ML, Jiang W, Bollinger JM. AurF from Streptomyces thioluteus and a possible new family of manganese/iron oxygenases. Biochemistry. 46: 10413-8. PMID 17718517 DOI: 10.1021/Bi701060G  0.826
2007 Eser BE, Barr EW, Frantom PA, Saleh L, Bollinger JM, Krebs C, Fitzpatrick PF. Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase. Journal of the American Chemical Society. 129: 11334-5. PMID 17715926 DOI: 10.1021/Ja074446S  0.788
2007 Jiang W, Hoffart LM, Krebs C, Bollinger JM. A manganese(IV)/iron(IV) intermediate in assembly of the manganese(IV)/iron(III) cofactor of Chlamydia trachomatis ribonucleotide reductase. Biochemistry. 46: 8709-16. PMID 17616152 DOI: 10.1021/Bi700906G  0.808
2007 Krebs C, Galonić Fujimori D, Walsh CT, Bollinger JM. Non-heme Fe(IV)-oxo intermediates. Accounts of Chemical Research. 40: 484-92. PMID 17542550 DOI: 10.1021/Ar700066P  0.822
2007 Jiang W, Bollinger JM, Krebs C. The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state. Journal of the American Chemical Society. 129: 7504-5. PMID 17530854 DOI: 10.1021/Ja072528A  0.781
2007 Jiang W, Yun D, Saleh L, Barr EW, Xing G, Hoffart LM, Maslak MA, Krebs C, Bollinger JM. A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase. Science (New York, N.Y.). 316: 1188-91. PMID 17525338 DOI: 10.1126/Science.1141179  0.774
2007 Sinnecker S, Svensen N, Barr EW, Ye S, Bollinger JM, Neese F, Krebs C. Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine: alpha-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant. Journal of the American Chemical Society. 129: 6168-79. PMID 17451240 DOI: 10.1021/Ja067899Q  0.779
2007 Ghiladi RA, Chufan EE, del Río D, Solomon EI, Krebs C, Huynh BH, Huang HW, Moënne-Loccoz P, Kaderli S, Honecker M, Zuberbühler AD, Marzilli L, Cotter RJ, Karlin KD. Further insights into the spectroscopic properties, electronic structure, and kinetics of formation of the heme-peroxo-copper complex [(F8TPP)FeIII-(O2(2-)-CuII(TMPA)]+. Inorganic Chemistry. 46: 3889-902. PMID 17444630 DOI: 10.1021/Ic061726K  0.433
2007 Behan RK, Hoffart LM, Stone KL, Krebs C, Green MT. Reaction of cytochrome P450BM3 and peroxynitrite yields nitrosyl complex. Journal of the American Chemical Society. 129: 5855-9. PMID 17432853 DOI: 10.1021/Ja064590Y  0.391
2007 Bollinger JM, Krebs C. Enzymatic C-H activation by metal-superoxo intermediates. Current Opinion in Chemical Biology. 11: 151-8. PMID 17374503 DOI: 10.1016/J.Cbpa.2007.02.037  0.745
2007 Galonić DP, Barr EW, Walsh CT, Bollinger JM, Krebs C. Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3. Nature Chemical Biology. 3: 113-6. PMID 17220900 DOI: 10.1038/Nchembio856  0.803
2006 Hoffart LM, Barr EW, Guyer RB, Bollinger JM, Krebs C. Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase. Proceedings of the National Academy of Sciences of the United States of America. 103: 14738-43. PMID 17003127 DOI: 10.1073/Pnas.0604005103  0.79
2006 Behan RK, Hoffart LM, Stone KL, Krebs C, Green MT. Evidence for basic ferryls in cytochromes P450. Journal of the American Chemical Society. 128: 11471-4. PMID 16939270 DOI: 10.1021/Ja062428P  0.325
2006 Kim SH, Xing G, Bollinger JM, Krebs C, Hoffman BM. Demonstration by 2H ENDOR spectroscopy that myo-inositol binds via an alkoxide bridge to the mixed-valent diiron center of myo-inositol oxygenase. Journal of the American Chemical Society. 128: 10374-5. PMID 16895396 DOI: 10.1021/Ja063602C  0.769
2006 Heinnickel M, Agalarov R, Svensen N, Krebs C, Golbeck JH. Identification of FX in the heliobacterial reaction center as a [4Fe-4S] cluster with an S = 3/2 ground spin state. Biochemistry. 45: 6756-64. PMID 16716087 DOI: 10.1021/Bi060031S  0.487
2006 Stone KL, Hoffart LM, Behan RK, Krebs C, Green MT. Evidence for two ferryl species in chloroperoxidase compound II. Journal of the American Chemical Society. 128: 6147-53. PMID 16669684 DOI: 10.1021/Ja057876W  0.411
2006 Xing G, Barr EW, Diao Y, Hoffart LM, Prabhu KS, Arner RJ, Reddy CC, Krebs C, Bollinger JM. Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol cleavage reaction catalyzed by myo-inositol oxygenase. Biochemistry. 45: 5402-12. PMID 16634621 DOI: 10.1021/bi0526276  0.775
2006 Xing G, Hoffart LM, Diao Y, Prabhu KS, Arner RJ, Reddy CC, Krebs C, Bollinger JM. A coupled dinuclear iron cluster that is perturbed by substrate binding in myo-inositol oxygenase. Biochemistry. 45: 5393-401. PMID 16634620 DOI: 10.1021/bi0519607  0.766
2006 Xing G, Diao Y, Hoffart LM, Barr EW, Prabhu KS, Arner RJ, Reddy CC, Krebs C, Bollinger JM. Evidence for C-H cleavage by an iron-superoxide complex in the glycol cleavage reaction catalyzed by myo-inositol oxygenase. Proceedings of the National Academy of Sciences of the United States of America. 103: 6130-5. PMID 16606846 DOI: 10.1073/Pnas.0508473103  0.782
2006 Bollinger JM, Krebs C. Stalking intermediates in oxygen activation by iron enzymes: motivation and method. Journal of Inorganic Biochemistry. 100: 586-605. PMID 16513177 DOI: 10.1016/J.Jinorgbio.2006.01.022  0.804
2006 Bollinger JMJ, Price JC, Hoffart LM, Barr EW, Krebs C. Mechanism of Taurine: α-Ketoglutarate Dioxygenase (TauD) from Escherichia coli Cheminform. 37. DOI: 10.1002/chin.200603269  0.641
2005 Smith AD, Jameson GN, Dos Santos PC, Agar JN, Naik S, Krebs C, Frazzon J, Dean DR, Huynh BH, Johnson MK. NifS-mediated assembly of [4Fe-4S] clusters in the N- and C-terminal domains of the NifU scaffold protein. Biochemistry. 44: 12955-69. PMID 16185064 DOI: 10.1021/Bi051257I  0.431
2005 Price JC, Barr EW, Hoffart LM, Krebs C, Bollinger JM. Kinetic dissection of the catalytic mechanism of taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry. 44: 8138-47. PMID 15924433 DOI: 10.1021/Bi050227C  0.778
2005 Cicchillo RM, Tu L, Stromberg JA, Hoffart LM, Krebs C, Booker SJ. Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. Journal of the American Chemical Society. 127: 7310-1. PMID 15898769 DOI: 10.1021/Ja051369X  0.474
2005 Krebs C, Price JC, Baldwin J, Saleh L, Green MT, Bollinger JM. Rapid freeze-quench 57Fe Mössbauer spectroscopy: monitoring changes of an iron-containing active site during a biochemical reaction. Inorganic Chemistry. 44: 742-57. PMID 15859243 DOI: 10.1021/Ic048523L  0.785
2005 Bollinger JM, Price JC, Hoffart LM, Barr EW, Krebs C. Mechanism of taurine: α-ketoglutarate dioxygenase (TauD) from Escherichia coli European Journal of Inorganic Chemistry. 4245-4254. DOI: 10.1002/Ejic.200500476  0.763
2004 Cicchillo RM, Lee KH, Baleanu-Gogonea C, Nesbitt NM, Krebs C, Booker SJ. Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide. Biochemistry. 43: 11770-81. PMID 15362861 DOI: 10.1021/Bi0488505  0.515
2004 Riggs-Gelasco PJ, Price JC, Guyer RB, Brehm JH, Barr EW, Bollinger JM, Krebs C. EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase. Journal of the American Chemical Society. 126: 8108-9. PMID 15225039 DOI: 10.1021/Ja048255Q  0.802
2004 Cicchillo RM, Baker MA, Schnitzer EJ, Newman EB, Krebs C, Booker SJ. Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis. The Journal of Biological Chemistry. 279: 32418-25. PMID 15155761 DOI: 10.1074/Jbc.M404381200  0.481
2004 Saleh L, Krebs C, Ley BA, Naik S, Huynh BH, Bollinger JM. Use of a chemical trigger for electron transfer to characterize a precursor to cluster X in assembly of the iron-radical cofactor of Escherichia coli ribonucleotide reductase. Biochemistry. 43: 5953-64. PMID 15147179 DOI: 10.1021/Bi036099E  0.801
2004 Cosper MM, Jameson GN, Hernández HL, Krebs C, Huynh BH, Johnson MK. Characterization of the cofactor composition of Escherichia coli biotin synthase. Biochemistry. 43: 2007-21. PMID 14967041 DOI: 10.1021/Bi0356653  0.469
2004 Tripp BC, Bell CB, Cruz F, Krebs C, Ferry JG. A role for iron in an ancient carbonic anhydrase. The Journal of Biological Chemistry. 279: 6683-7. PMID 14662760 DOI: 10.1074/Jbc.M311648200  0.514
2003 Hurshman AR, Krebs C, Edmondson DE, Marletta MA. Ability of tetrahydrobiopterin analogues to support catalysis by inducible nitric oxide synthase: formation of a pterin radical is required for enzyme activity. Biochemistry. 42: 13287-303. PMID 14609340 DOI: 10.1021/Bi035491P  0.314
2003 Baldwin J, Krebs C, Saleh L, Stelling M, Huynh BH, Bollinger JM, Riggs-Gelasco P. Structural characterization of the peroxodiiron(III) intermediate generated during oxygen activation by the W48A/D84E variant of ribonucleotide reductase protein R2 from Escherichia coli. Biochemistry. 42: 13269-79. PMID 14609338 DOI: 10.1021/Bi035198P  0.795
2003 Price JC, Barr EW, Glass TE, Krebs C, Bollinger JM. Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:alpha-ketoglutarate dioxygenase (TauD). Journal of the American Chemical Society. 125: 13008-9. PMID 14570457 DOI: 10.1021/Ja037400H  0.79
2003 Price JC, Barr EW, Tirupati B, Bollinger JM, Krebs C. The first direct characterization of a high-valent iron intermediate in the reaction of an alpha-ketoglutarate-dependent dioxygenase: a high-spin FeIV complex in taurine/alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry. 42: 7497-508. PMID 12809506 DOI: 10.1021/Bi030011F  0.821
2003 Price JC, Barr EW, Tirupati B, Bollinger J, Krebs C. On the identity of a novel Fe(IV) intermediate in the catalytic cycle of taurine alpha-ketoglutarate dioxygenase Journal of Inorganic Biochemistry. 96: 212. DOI: 10.1016/S0162-0134(03)80742-0  0.742
2003 Bollinger J, Price JC, Barr EW, Tirupati B, Krebs C. Characterization of a high-spin Fe(IV) intermediate in the reaction of taurine/alpha-ketoglutarate dioxygenase (TauD) Journal of Inorganic Biochemistry. 96: 63. DOI: 10.1016/S0162-0134(03)80511-1  0.734
2003 Chaudhuri P, Rentschler E, Birkelbach F, Krebs C, Bill E, Weyhermüller T, Flörke U. Ground Spin State Variation in Carboxylate-Bridged Tetranuclear [Fe2Mn2O2]8+ Cores and a Comparison with Their [Fe4O2]8+ and [Mn4O2]8+ Congeners European Journal of Inorganic Chemistry. 2003: 541-555. DOI: 10.1002/Ejic.200390076  0.407
2002 Krebs C, Edmondson DE, Huynh BH. Demonstration of peroxodiferric intermediate in M-ferritin ferroxidase reaction using rapid freeze-quench Mössbauer, resonance Raman, and XAS spectroscopies. Methods in Enzymology. 354: 436-54. PMID 12418245 DOI: 10.1016/S0076-6879(02)54034-9  0.387
2002 Jameson GN, Jin W, Krebs C, Perreira AS, Tavares P, Liu X, Theil EC, Huynh BH. Stoichiometric production of hydrogen peroxide and parallel formation of ferric multimers through decay of the diferric-peroxo complex, the first detectable intermediate in ferritin mineralization. Biochemistry. 41: 13435-43. PMID 12416989 DOI: 10.1021/Bi026478S  0.396
2002 Krebs C, Bollinger JM, Theil EC, Huynh BH. Exchange coupling constant J of peroxodiferric reaction intermediates determined by Mössbauer spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 7: 863-9. PMID 12203023 DOI: 10.1007/S00775-002-0371-1  0.736
2002 Lee D, Pierce B, Krebs C, Hendrich MP, Huynh BH, Lippard SJ. Functional mimic of dioxygen-activating centers in non-heme diiron enzymes: mechanistic implications of paramagnetic intermediates in the reactions between diiron(II) complexes and dioxygen. Journal of the American Chemical Society. 124: 3993-4007. PMID 11942838 DOI: 10.1021/Ja012251T  0.57
2002 Krebs C, Broderick WE, Henshaw TF, Broderick JB, Huynh BH. Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: a Mössbauer spectroscopic study. Journal of the American Chemical Society. 124: 912-3. PMID 11829592 DOI: 10.1021/Ja017562I  0.555
2002 Yun D, Krebs C, Gupta GP, Iwig DF, Huynh BH, Bollinger JM. Facile electron transfer during formation of cluster X and kinetic competence of X for tyrosyl radical production in protein R2 of ribonucleotide reductase from mouse. Biochemistry. 41: 981-90. PMID 11790122 DOI: 10.1021/Bi011797P  0.772
2001 Krebs C, Agar JN, Smith AD, Frazzon J, Dean DR, Huynh BH, Johnson MK. IscA, an alternate scaffold for Fe-S cluster biosynthesis. Biochemistry. 40: 14069-80. PMID 11705400 DOI: 10.1021/Bi015656Z  0.473
2001 Baldwin J, Voegtli WC, Khidekel N, Moënne-Loccoz P, Krebs C, Pereira AS, Ley BA, Huynh BH, Loehr TM, Riggs-Gelasco PJ, Rosenzweig AC, Bollinger JM. Rational reprogramming of the R2 subunit of Escherichia coli ribonucleotide reductase into a self-hydroxylating monooxygenase. Journal of the American Chemical Society. 123: 7017-30. PMID 11459480 DOI: 10.1021/Ja002114G  0.831
2000 Agar JN, Krebs C, Frazzon J, Huynh BH, Dean DR, Johnson MK. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry. 39: 7856-62. PMID 10891064 DOI: 10.1021/Bi000931N  0.455
2000 Jovanović T, Ascenso C, Hazlett KR, Sikkink R, Krebs C, Litwiller R, Benson LM, Moura I, Moura JJ, Radolf JD, Huynh BH, Naylor S, Rusnak F. Neelaredoxin, an iron-binding protein from the syphilis spirochete, Treponema pallidum, is a superoxide reductase. The Journal of Biological Chemistry. 275: 28439-48. PMID 10874033 DOI: 10.1074/Jbc.M003314200  0.435
2000 Hwang J, Krebs C, Huynh BH, Edmondson DE, Theil EC, Penner-Hahn JE. A short Fe-Fe distance in peroxodiferric ferritin: control of Fe substrate versus cofactor decay? Science (New York, N.Y.). 287: 122-5. PMID 10615044 DOI: 10.1126/Science.287.5450.122  0.559
2000 Lee D, Krebs C, Huynh BH, Hendrich MP, Lippard SJ. Valence-delocalized diiron(II,III) cores supported by carboxylate-only bridging ligands [11] Journal of the American Chemical Society. 122: 5000-5001. DOI: 10.1021/Ja994448F  0.571
2000 Krebs C, Henshaw TF, Cheek J, Huynh BH, Broderick JB. Conversion of 3Fe-4S to 4Fe-4S clusters in native pyruvate formate-lyase activating enzyme: Mössbauer characterization and implications for mechanism Journal of the American Chemical Society. 122: 12497-12506. DOI: 10.1021/Ja003335P  0.51
2000 Krebs C, Chen S, Baldwin J, Ley BA, Patel U, Edmondson DE, Huynh BH, Bollinger JM. Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 2. Evidence for and consequences of blocked electron transfer in the W48F variant Journal of the American Chemical Society. 122: 12207-12219. DOI: 10.1021/Ja001279M  0.762
2000 Baldwin J, Krebs C, Ley BA, Edmondson DE, Huynh BH, Bollinger JM. Mechanism of rapid electron transfer during oxygen activation in the R2 subunit of Escherichia coli ribonucleotide reductase. 1. Evidence for a transient tryptophan radical Journal of the American Chemical Society. 122: 12195-12206. DOI: 10.1021/Ja001278U  0.771
2000 Krebs C, Davydov R, Baldwin J, Hoffman BM, Bollinger JM, Huynh BH. Mossbauer and EPR characterization of the S = 9/2 mixed-valence Fe(II)Fe(III) cluster in the cryoreduced R2 subunit of Escherichia coli ribonucleotide reductase Journal of the American Chemical Society. 122: 5327-5336. DOI: 10.1021/Ja000317Z  0.746
2000 Nasri H, Ellison MK, Krebs C, Huynh BH, Scheidt WR. Highly variable π-bonding in the interaction of iron(II) porphyrinates with nitrite Journal of the American Chemical Society. 122: 10795-10804. DOI: 10.1021/Ja000149A  0.538
1999 Krebs C, Glaser T, Bill E, Weyhermüller T, Meyer-Klaucke W, Wieghardt K. A Paramagnetic Copper(III) Complex Containing an Octahedral Cu S Coordination Polyhedron. Angewandte Chemie (International Ed. in English). 38: 359-361. PMID 29711643 DOI: 10.1002/(Sici)1521-3773(19990201)38:3<359::Aid-Anie359>3.0.Co;2-5  0.634
1999 Hurshman AR, Krebs C, Edmondson DE, Huynh BH, Marletta MA. Formation of a pterin radical in the reaction of the heme domain of inducible nitric oxide synthase with oxygen. Biochemistry. 38: 15689-96. PMID 10625434 DOI: 10.1021/Bi992026C  0.374
1999 Pereira AS, Tavares P, Krebs C, Huynh BH, Rusnak F, Moura I, Moura JJ. Biochemical and spectroscopic characterization of overexpressed fuscoredoxin from Escherichia coli. Biochemical and Biophysical Research Communications. 260: 209-15. PMID 10381368 DOI: 10.1006/Bbrc.1999.0748  0.429
1999 Moënne-Loccoz P, Krebs C, Herlihy K, Edmondson DE, Theil EC, Huynh BH, Loehr TM. The ferroxidase reaction of ferritin reveals a diferric mu-1,2 bridging peroxide intermediate in common with other O2-activating non-heme diiron proteins. Biochemistry. 38: 5290-5. PMID 10220314 DOI: 10.1021/Bi990095L  0.555
1999 Lee D, Du Bois J, Petasis D, Hendrich MP, Krebs C, Huynh BH, Lippard SJ. Formation of Fe(III)Fe(IV) species from the reaction between a diiron(II) complex and dioxygen: Relevance to ribonucleotide reductase intermediate X [12] Journal of the American Chemical Society. 121: 9893-9894. DOI: 10.1021/Ja9923686  0.43
1999 Krebs C, Glaser T, Bill E, Weyhermüller T, Meyer-Klaucke W, Wieghardt K. Ein paramagnetischer Kupfer(III)-Komplex mit oktaedrischem CuIIIS6-Koordinationspolyeder Angewandte Chemie. 111: 370-372. DOI: 10.1002/(Sici)1521-3757(19990201)111:3<370::Aid-Ange370>3.0.Co;2-Y  0.667
1998 Pereira AS, Small W, Krebs C, Tavares P, Edmondson DE, Theil EC, Huynh BH. Direct spectroscopic and kinetic evidence for the involvement of a peroxodiferric intermediate during the ferroxidase reaction in fast ferritin mineralization. Biochemistry. 37: 9871-6. PMID 9665690 DOI: 10.1021/Bi980847W  0.472
1998 Tavares P, Pereira AS, Krebs C, Ravi N, Moura JJ, Moura I, Huynh BH. Spectroscopic characterization of a novel tetranuclear Fe cluster in an iron-sulfur protein isolated from Desulfovibrio desulfuricans. Biochemistry. 37: 2830-42. PMID 9485434 DOI: 10.1021/Bi9723008  0.473
1998 Valentine AM, Tavares P, Pereira AS, Davydov R, Krebs C, Hoffman BM, Edmondson DE, Boi Hanh Huynh, Lippard SJ. Generation of a mixed-valent Fe(III)Fe(IV) form of intermediate Q in the reaction cycle of soluble methane monooxygenase, an analog of intermediate X in ribonucleotide reductase R2 assembly [10] Journal of the American Chemical Society. 120: 2190-2191. DOI: 10.1021/Ja974169X  0.507
1998 Bollinger J.M. J, Krebs C, Vicol A, Chen S, Ley BA, Edmondson DE, Huynh BH. Engineering the diiron site of Escherichia coli ribonucleotide reductase protein R2 to accumulate an intermediate similar to H(peroxo), the putative peroxodiiron(III) complex from the methane monooxygenase catalytic cycle [13] Journal of the American Chemical Society. 120: 1094-1095. DOI: 10.1021/Ja973651C  0.373
1997 Bossek U, Nühlen D, Bill E, Glaser T, Krebs C, Weyhermüller T, Wieghardt K, Lengen M, Trautwein AX. Exchange Coupling in an Isostructural Series of Face-Sharing Bioctahedral Complexes [LM(II)(&mgr;-X)(3)M(II)L]BPh(4) (M = Mn, Fe, Co, Ni, Zn; X = Cl, Br; L = 1,4,7-Trimethyl-1,4,7-triazacyclononane). Inorganic Chemistry. 36: 2834-2843. PMID 11669919 DOI: 10.1021/Ic970119H  0.671
1996 Beissel T, Birkelbach F, Bill E, Glaser T, Kesting F, Krebs C, Weyhermüller T, Wieghardt K, Butzlaff C, Trautwein AX. Exchange and Double-Exchange Phenomena in Linear Homo- and Heterotrinuclear Nickel(II,III,IV) Complexes Containing Six μ2-Phenolato or μ2-Thiophenolato Bridging Ligands Journal of the American Chemical Society. 118: 12376-12390. DOI: 10.1021/Ja961305+  0.631
1995 Krebs C, Winter M, Weyhermüller T, Bill E, Wieghardt K, Chaudhuri P. Magnetic exchange coupling in a nearly linear iron(III)nickel(II)nickel(II)iron(III) complex Journal of the Chemical Society, Chemical Communications. 1913-1915. DOI: 10.1039/C39950001913  0.6
1995 Krebs C, Winter M, Weyhermüller T, Bill E, Wieghardt K, Chaudhuri P. A novel linear hetero-tetranuclear complex, FeIIINiIINiIIFeIII Journal of Inorganic Biochemistry. 59: 342. DOI: 10.1016/0162-0134(95)97441-R  0.444
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