| 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 |
0.705 |
|
| 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 |
0.657 |
|
| 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 |
0.841 |
|
| 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 |
0.695 |
|
| 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 |
0.715 |
|
| 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 |
0.824 |
|
| 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 |
0.851 |
|
| 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 |
0.708 |
|
| 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 |
0.764 |
|
| 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 |
0.731 |
|
| 2021 |
McBride MJ, Pope SR, Hu K, Okafor CD, Balskus EP, Bollinger JM, Boal AK. Structure and assembly of the diiron cofactor in the heme-oxygenase-like domain of the -nitrosourea-producing enzyme SznF. Proceedings of the National Academy of Sciences of the United States of America. 118. PMID 33468680 DOI: 10.1073/pnas.2015931118 |
0.673 |
|
| 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 |
0.807 |
|
| 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 |
0.672 |
|
| 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 |
0.848 |
|
| 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 |
0.641 |
|
| 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 |
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 |
0.85 |
|
| 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 |
0.863 |
|
| 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 |
0.846 |
|
| 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 |
0.828 |
|
| 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 |
0.847 |
|
| 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 |
|
| 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 |
0.747 |
|
| 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, ... Bollinger JM, 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 |
0.765 |
|
| 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 |
0.81 |
|
| 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 |
0.844 |
|
| 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 |
0.803 |
|
| 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, et al. The biosynthesis of methanobactin. Science (New York, N.Y.). 359: 1411-1416. PMID 29567715 DOI: 10.1126/Science.Aap9437 |
0.795 |
|
| 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 |
0.723 |
|
| 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 |
0.861 |
|
| 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 |
0.854 |
|
| 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 |
0.707 |
|
| 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, ... ... Bollinger JM, 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 |
0.753 |
|
| 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 |
0.814 |
|
| 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 |
0.861 |
|
| 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 |
0.693 |
|
| 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 |
0.803 |
|
| 2015 |
Boal AK, Bollinger JM, Chang WC. Assembly of the unusual oxacycles in the orthosomycin antibiotics. Proceedings of the National Academy of Sciences of the United States of America. 112: 11989-90. PMID 26378126 DOI: 10.1073/Pnas.1514689112 |
0.346 |
|
| 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 |
0.831 |
|
| 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 |
0.828 |
|
| 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 |
0.847 |
|
| 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 |
0.774 |
|
| 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 |
0.822 |
|
| 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 |
0.817 |
|
| 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 |
0.803 |
|
| 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 |
0.74 |
|
| 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, 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 |
0.851 |
|
| 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 |
0.78 |
|
| 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 |
0.856 |
|
| 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 |
0.728 |
|
| 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, ... ... Bollinger JM, et al. The COMBREX project: design, methodology, and initial results. Plos Biology. 11: e1001638. PMID 24013487 DOI: 10.1371/Journal.Pbio.1001638 |
0.537 |
|
| 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 |
0.858 |
|
| 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 |
0.84 |
|
| 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 |
0.817 |
|
| 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 |
0.831 |
|
| 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 |
0.854 |
|
| 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 |
0.752 |
|
| 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 |
0.707 |
|
| 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 |
0.803 |
|
| 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 |
0.845 |
|
| 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 |
0.784 |
|
| 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 |
0.796 |
|
| 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 |
0.758 |
|
| 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 |
0.746 |
|
| 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 |
0.805 |
|
| 2010 |
Hollenhorst MA, Bumpus SB, Matthews ML, Bollinger JM, Kelleher NL, Walsh CT. The nonribosomal peptide synthetase enzyme DdaD tethers N(β)-fumaramoyl-l-2,3-diaminopropionate for Fe(II)/α-ketoglutarate-dependent epoxidation by DdaC during dapdiamide antibiotic biosynthesis. Journal of the American Chemical Society. 132: 15773-81. PMID 20945916 DOI: 10.1021/Ja1072367 |
0.808 |
|
| 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 |
0.628 |
|
| 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 |
0.681 |
|
| 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 |
0.721 |
|
| 2010 |
Bollinger JM, Matthews ML. Biochemistry. Remote enzyme microsurgery. Science (New York, N.Y.). 327: 1337-8. PMID 20223975 DOI: 10.1126/Science.1187421 |
0.572 |
|
| 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 |
0.756 |
|
| 2009 |
Behshad E, Bollinger JM. Kinetic analysis of cysteine desulfurase CD0387 from Synechocystis sp. PCC 6803: formation of the persulfide intermediate. Biochemistry. 48: 12014-23. PMID 19883076 DOI: 10.1021/Bi802161U |
0.8 |
|
| 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 |
0.85 |
|
| 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 |
0.727 |
|
| 2009 |
Meneely KM, Barr EW, Bollinger JM, Lamb AL. Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction. Biochemistry. 48: 4371-6. PMID 19368334 DOI: 10.1021/Bi900442Z |
0.306 |
|
| 2009 |
Bollinger JM, Broderick JB. Frontiers in enzymatic C-H-bond activation. Current Opinion in Chemical Biology. 13: 51-7. PMID 19362514 DOI: 10.1016/J.Cbpa.2009.03.018 |
0.562 |
|
| 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 |
0.81 |
|
| 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 |
0.717 |
|
| 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 |
0.813 |
|
| 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 |
0.734 |
|
| 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 |
0.707 |
|
| 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 |
0.711 |
|
| 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 |
0.703 |
|
| 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 |
0.734 |
|
| 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 |
0.81 |
|
| 2007 |
Yun D, Saleh L, García-Serres R, Chicalese BM, An YH, Huynh BH, Bollinger JM. Addition of oxygen to the diiron(II/II) cluster is the slowest step in formation of the tyrosyl radical in the W103Y variant of ribonucleotide reductase protein R2 from mouse. Biochemistry. 46: 13067-73. PMID 17941645 DOI: 10.1021/bi7003747 |
0.356 |
|
| 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 |
0.847 |
|
| 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 |
0.788 |
|
| 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 |
0.724 |
|
| 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 |
0.746 |
|
| 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 |
0.798 |
|
| 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 |
0.714 |
|
| 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 |
0.713 |
|
| 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 |
0.713 |
|
| 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 |
0.675 |
|
| 2007 |
Yun D, García-Serres R, Chicalese BM, An YH, Huynh BH, Bollinger JM. (Mu-1,2-peroxo)diiron(III/III) complex as a precursor to the diiron(III/IV) intermediate X in the assembly of the iron-radical cofactor of ribonucleotide reductase from mouse. Biochemistry. 46: 1925-32. PMID 17256972 DOI: 10.1021/bi061717n |
0.448 |
|
| 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 |
0.779 |
|
| 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 |
0.728 |
|
| 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 |
0.702 |
|
| 2006 |
Yeh E, Cole LJ, Barr EW, Bollinger JM, Ballou DP, Walsh CT. Flavin redox chemistry precedes substrate chlorination during the reaction of the flavin-dependent halogenase RebH. Biochemistry. 45: 7904-12. PMID 16784243 DOI: 10.1021/Bi060607D |
0.637 |
|
| 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 |
0.732 |
|
| 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 |
0.716 |
|
| 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 |
0.719 |
|
| 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 |
0.746 |
|
| 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 |
0.581 |
|
| 2005 |
Sommerhalter M, Saleh L, Bollinger JM, Rosenzweig AC. Structure of Escherichia coli ribonucleotide reductase R2 in space group P6122. Acta Crystallographica. Section D, Biological Crystallography. 61: 1649-54. PMID 16301799 DOI: 10.1107/S0907444905034062 |
0.51 |
|
| 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 |
0.713 |
|
| 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 |
0.718 |
|
| 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 |
0.699 |
|
| 2004 |
Behshad E, Parkin SE, Bollinger JM. Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: kinetic analysis of cleavage of the persulfide intermediate by chemical reductants. Biochemistry. 43: 12220-6. PMID 15379560 DOI: 10.1021/Bi049143E |
0.789 |
|
| 2004 |
Lu S, Libby E, Saleh L, Xing G, Bollinger JM, Moënne-Loccoz P. Characterization of NO adducts of the diiron center in protein R2 of Escherichia coli ribonucleotide reductase and site-directed variants; implications for the O2 activation mechanism. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 9: 818-27. PMID 15311337 DOI: 10.1007/S00775-004-0582-8 |
0.406 |
|
| 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 |
0.856 |
|
| 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 |
0.741 |
|
| 2004 |
Saleh L, Kelch BA, Pathickal BA, Baldwin J, Ley BA, Bollinger JM. Mediation by indole analogues of electron transfer during oxygen activation in variants of Escherichia coli ribonucleotide reductase R2 lacking the electron-shuttling tryptophan 48. Biochemistry. 43: 5943-52. PMID 15147178 DOI: 10.1021/Bi036098M |
0.402 |
|
| 2003 |
Voegtli WC, Sommerhalter M, Saleh L, Baldwin J, Bollinger JM, Rosenzweig AC. Variable coordination geometries at the diiron(II) active site of ribonucleotide reductase R2. Journal of the American Chemical Society. 125: 15822-30. PMID 14677973 DOI: 10.1021/Ja0370387 |
0.622 |
|
| 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 |
0.853 |
|
| 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 |
0.727 |
|
| 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 |
0.766 |
|
| 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 |
0.665 |
|
| 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 |
0.655 |
|
| 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 |
0.662 |
|
| 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 |
0.707 |
|
| 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 |
0.848 |
|
| 2000 |
Voegtli WC, Khidekel N, Baldwin J, Ley BA, Bollinger JM, Rosenzweig AC. Crystal structure of the ribonucleotide reductase R2 mutant that accumulates a μ-1,2-peroxodiiron(III) intermediate during oxygen activation Journal of the American Chemical Society. 122: 3255-3261. DOI: 10.1021/Ja991839L |
0.589 |
|
| 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 |
0.696 |
|
| 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 |
0.706 |
|
| 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 |
0.673 |
|
| 1998 |
Moënne-Loccoz P, Baldwin J, Ley BA, Loehr TM, Bollinger JM. O2 activation by non-heme diiron proteins: identification of a symmetric mu-1,2-peroxide in a mutant of ribonucleotide reductase. Biochemistry. 37: 14659-63. PMID 9778340 DOI: 10.1021/bi981838q |
0.439 |
|
| 1998 |
Parkin SE, Chen S, Ley BA, Mangravite L, Edmondson DE, Huynh BH, Bollinger JM. Electron injection through a specific pathway determines the outcome of oxygen activation at the diiron cluster in the F208Y mutant of Escherichia coli ribonucleotide reductase protein R2. Biochemistry. 37: 1124-30. PMID 9454605 DOI: 10.1021/Bi9723717 |
0.355 |
|
| 1997 |
Lin CH, Kwon DS, Bollinger JM, Walsh CT. Evidence for a glutathionyl-enzyme intermediate in the amidase activity of the bifunctional glutathionylspermidine synthetase/amidase from Escherichia coli. Biochemistry. 36: 14930-8. PMID 9398217 DOI: 10.1021/bi9714464 |
0.435 |
|
| 1997 |
Kwon DS, Lin CH, Chen S, Coward JK, Walsh CT, Bollinger JM. Dissection of glutathionylspermidine synthetase/amidase from Escherichia coli into autonomously folding and functional synthetase and amidase domains. The Journal of Biological Chemistry. 272: 2429-36. PMID 8999955 DOI: 10.1074/jbc.272.4.2429 |
0.427 |
|
| 1995 |
Bollinger JM, Tong WH, Ravi N, Huynh BH, Edmondson DE, Stubbe JA. Use of rapid kinetics methods to study the assembly of the diferric-tyrosyl radical cofactor of E. coli ribonucleotide reductase. Methods in Enzymology. 258: 278-303. PMID 8524156 DOI: 10.1016/0076-6879(95)58052-2 |
0.634 |
|
| 1995 |
Bollinger JM, Kwon DS, Huisman GW, Kolter R, Walsh CT. Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase. The Journal of Biological Chemistry. 270: 14031-41. PMID 7775463 DOI: 10.1074/Jbc.270.23.14031 |
0.471 |
|
| 1995 |
Hidalgo E, Bollinger JM, Bradley TM, Walsh CT, Demple B. Binuclear [2Fe-2S] clusters in the Escherichia coli SoxR protein and role of the metal centers in transcription. The Journal of Biological Chemistry. 270: 20908-14. PMID 7673113 DOI: 10.1074/Jbc.270.36.20908 |
0.55 |
|
| 1995 |
Pulver SC, Tong WH, Bollinger JM, Stubbe J, Solomon EI. Circular dichroism and magnetic circular dichroism studies of the fully reduced binuclear non-heme iron active site in the Escherichia coli R2 subunit of ribonucleoside diphosphate reductase Journal of the American Chemical Society. 117: 12664-12678. DOI: 10.1021/Ja00156A002 |
0.685 |
|
| 1994 |
Bollinger JM, Tong WH, Ravi N, Huynh BH, Edmondson DE, Stubbe J. Mechanism of Assembly of the Tyrosyl Radical-Diiron(III) Cofactorof E. coli Ribonucleotide Reductase. 3. Kinetics of the Limiting Fe2+ Reaction by Optical, EPR, and Moessbauer Spectroscopies Journal of the American Chemical Society. 116: 8024-8032. DOI: 10.1021/Ja00097A009 |
0.68 |
|
| 1994 |
Ravi N, Bollinger JM, Huynh BH, Stubbe J, Edmondson DE. Mechanism of Assembly of the Tyrosyl Radical-Diiron(III) Cofactor of E. Coli Ribonucleotide Reductase: 1. Moessbauer Characterization of the Diferric Radical Precursor Journal of the American Chemical Society. 116: 8007-8014. DOI: 10.1021/Ja00097A007 |
0.627 |
|
| 1993 |
Salowe S, Bollinger JM, Ator M, Stubbe J, McCraken J, Peisach J, Samano MC, Robins MJ. Alternative model for mechanism-based inhibition of Escherichia coli ribonucleotide reductase by 2'-azido-2'-deoxyuridine 5'-diphosphate. Biochemistry. 32: 12749-60. PMID 8251496 DOI: 10.1021/Bi00210A026 |
0.64 |
|
| 1993 |
Gerfen GJ, Bellew BF, Un S, Bollinger JM, Stubbe J, Griffin RG, Singel DJ. High-frequency (139.5 GHz) EPR spectroscopy of the tyrosyl radical in Escherichia coli ribonucleotide reductase Journal of the American Chemical Society. 115: 6420-6421. DOI: 10.1021/Ja00067A071 |
0.576 |
|
| 1993 |
Ravi N, Bollinger J, Tong W, Edmondson D, Stubbe J, Huynh B. A Mössbauer investigation of the kinetic intermediates involved in formation of the tyrosyl radical-diferric center cofactor in E. Coli ribonucleotide reductase Journal of Inorganic Biochemistry. 51: 276. DOI: 10.1016/0162-0134(93)85308-U |
0.618 |
|
| 1993 |
Bollinger J, Ravi N, Tong W, Edmondson D, Huynh B, Stubbe J. Assembly of the iron center-tyrosyl radical cofactor of ribonucleotide reductase Journal of Inorganic Biochemistry. 51: 6. DOI: 10.1016/0162-0134(93)85045-A |
0.648 |
|
| 1992 |
Mao SS, Holler TP, Yu GX, Bollinger JM, Booker S, Johnston MI, Stubbe J. A model for the role of multiple cysteine residues involved in ribonucleotide reduction: amazing and still confusing. Biochemistry. 31: 9733-43. PMID 1382592 |
0.589 |
|
| 1991 |
Baker CH, Banzon J, Bollinger JM, Stubbe J, Samano V, Robins MJ, Lippert B, Jarvi E, Resvick R. 2'-Deoxy-2'-methylenecytidine and 2'-deoxy-2',2'-difluorocytidine 5'-diphosphates: potent mechanism-based inhibitors of ribonucleotide reductase. Journal of Medicinal Chemistry. 34: 1879-84. PMID 2061926 DOI: 10.1021/Jm00110A019 |
0.618 |
|
| 1991 |
Bollinger JM, Edmondson DE, Huynh BH, Filley J, Norton JR, Stubbe J. Mechanism of assembly of the tyrosyl radical-dinuclear iron cluster cofactor of ribonucleotide reductase. Science (New York, N.Y.). 253: 292-8. PMID 1650033 DOI: 10.1126/Science.1650033 |
0.711 |
|
| 1991 |
Bollinger JM, Stubbe J, Huynh BH, Edmondson DE. Novel diferric radical intermediate responsible for tyrosyl radical formation in assembly of the cofactor of ribonucleotide reductase Journal of the American Chemical Society. 113: 6289-6291. DOI: 10.1021/Ja00016A066 |
0.594 |
|
| 1989 |
Mao SS, Johnston MI, Bollinger JM, Stubbe J. Mechanism-based inhibition of a mutant Escherichia coli ribonucleotide reductase (cysteine-225----serine) by its substrate CDP. Proceedings of the National Academy of Sciences of the United States of America. 86: 1485-9. PMID 2493643 DOI: 10.1073/Pnas.86.5.1485 |
0.59 |
|
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