Carsten Krebs - Publications

Affiliations: 
Pennsylvania State University, State College, PA, United States 
Area:
Biochemistry
Website:
http://sites.psu.edu/bollingerkrebsgroup/carsten-krebs/

72 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
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  0.6
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  0.72
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  0.36
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  0.6
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  0.6
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2008 Krebs C, Huynh BH. Intermediates in oxygen activation reactions of diiron enzymes Iron Metabolism: Inorganic Biochemistry and Regulatory Mechanisms. 253-273. DOI: 10.1002/9783527613700.ch16  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
2001 Ghiladi RA, Hatwell KR, Karlin KD, Huang HW, Moënne-Loccoz P, Krebs C, Huynh BH, Marzilli LA, Cotter RJ, Kaderli S, Zuberbühler AD. Dioxygen reactivity of mononuclear heme and copper components yielding a high-spin heme-peroxo-cu complex. Journal of the American Chemical Society. 123: 6183-4. PMID 11414855 DOI: 10.1021/Ja010602Y  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.92
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.72
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  0.92
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