Publications by Carsten Krebs

2007

Galonic, D. P., E. W. Barr, C. T. Walsh, J. M. Bollinger, Jr., and C. Krebs.  Two interconverting Fe(IV) intermediates in aliphatic chlorination by the halogenase CytC3.  Nat. Chem. Biol. 3:113-116.

Bollinger, J. M., Jr. and C. Krebs.  Enzymatic C-H activation by metal-superoxo intermediates.  Curr. Opin. Chem. Biol. 11:151-158.

Behan, R. K., L. M. Hoffart, K. L. Stone, C. Krebs, and M. T. Green.  Reaction between cytochrome P450BM3 and peroxynitrite yields nitrosyl complex.  J. Am. Chem. Soc. 129:5855-5859.

Ghiladi, R., E. Chufan, D. del Rio, E. I. Solomon, C. Krebs, B.-H. Huynh, H.-W. Huang, P. Moënne-Loccoz, S. Kaderli, M. Honecker, A. Zuberbühler, L. Marzilli, R. Cotter, and K. D.  Karlin.  Further insights into the spectroscopic properties, electronic structure and kinetics of formation of the heme-peroxo-copper complex [(F8TPP)FeIII μ-(O22-)-CuII(TMPA)].  Inorg. Chem. 46:3889-3902.

Sinnecker, S., N. Svensen, E. W. Barr, S. Ye, J. M. Bollinger, Jr., F. Neese, and C. Krebs.

Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-Oxo intermediates in taurine:a-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant.  J. Am. Chem. Soc. 129:6168-6179.

Jiang, W., D. Yun, L. Saleh, E. W. Barr, G. Xing, L. M. Hoffart, M. A. Maslak, C. Krebs, and  J. M. Bollinger, Jr.  A manganese(IV)/iron(III) cofactor in Chlamydia trachomatis ribonucleotide reductase.  Science 316:1188-1191.

Jiang, W., J. M. Bollinger, Jr., and C. Krebs.  The active form of Chlamydia trachomatis ribonucleotide reductase R2 protein contains a heterodinuclear Mn(IV)/Fe(III) cluster with S = 1 ground state.  J. Am. Chem. Soc. 129:7504-7505.

Krebs, C., D. G. Fujimori, C. T. Walsh, and J. M. Bollinger, Jr.  Non-heme Fe(IV)-oxo intermediates.  Acc. Chem. Res. 40:484-492.

Jiang, W., L. M. Hoffart, C. Krebs, and J. M. Bollinger, Jr.  A Mn(IV)/Fe(IV) intermediate in assembly of the Mn(IV)/Fe(III) cofactor of Chlamydia trachomatis ribonucleotide reductase.  Biochemistry 46:8709-8716.

Krebs, C., M. L. Matthews, W. Jiang, and J. M. Bollinger, Jr.  AurF from Streptomyces thioluteus and a possible new family of manganese/iron oxygenases.  Biochemistry 46:10413-10418.

Wu, C.-H., W. Jiang, C. Krebs, and J. Stubbe.  YfaE, a ferredoxin involved in diferric-tyrosyl radical maintenance in E. coli ribonucleotide reductase.  Biochemistry 46:11577-11588.

Eser, B., E. W. Barr, P. A. Frantom, L. Saleh, J. M. Bollinger, Jr., C. Krebs, and P. F. Fitzpatrick.  Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase.  J. Am. Chem. Soc. 129:11334-11335.

Shen, G., R. Balasubramanian, T. Wang, Y. Wu, L. M. Hoffart, C. Krebs, D. A. Bryant, and J. H. Golbeck.  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.  J. Biol. Chem. 282:31909-31919.

Fujimori, D. G., E. W. Barr, M. L. Matthews, G. M. Koch, J. R. Yonce, C. T. Walsh, J. M. Bollinger, Jr., C. Krebs, and P. J. Riggs-Gelasco.  Spectroscopic evidence for a high-spin Br- Fe(IV)-oxo intermediate in the α-ketoglutarate-dependent halogenase CytC3 from Streptomyces.  J. Am. Chem. Soc. 129:13408-13409.

Neidig, M. L., C. D. Brown, K. M. Light, D. G. Fujimori, E. M. Nolan, J. C. Price, E. W. Barr, J. M. Bollinger, Jr., C. Krebs, C. T. Walsh, and E. I. Solomon.  CD and MCD of CytC3 and taurine dioxygenase: Role of the facial triad in α-KG-dependent dioxygenases.  J. Am. Chem. Soc. 129:14224-14231.

2006

Hoffart, L. M., E. W. Barr, R. B. Guyer, J. M. Bollinger, Jr., and C. Krebs.  Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a Prolyl-4-hydroxylase.  Proc. Natl. Acad. Sci. USA 103:14738-14743.

Kim, S. H., G. Xing, J. M. Bollinger, Jr., C. Krebs, and B. M. Hoffman.  Demonstration by 2H ENDOR spectroscopy that myo-inositol binds via an alkoxide bridge to the mixed-valent diiron center of myo-inositol oxygenase.  J. Am. Chem. Soc. 128:10374-10375.

Xing, G., Y. Diao, L. M. Hoffart, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr.  Novel mechanisms of oxygen activation and C-H cleavage by a dinuclear iron cluster in myo-inositol oxygenase.  Proc. Natl. Acad. Sci. USA 103:6130-6135.

Xing, G., L. M. Hoffart, Y. Diao, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr.  Oxygen activation by a mixed-valent, diiron(II/III) cluster in the glycol-cleavage reaction catalyzed by myo-inositol oxygenase.  Biochemistry 45:5402-5412.

Xing, G., L. M. Hoffart, Y. Diao, S. Prabhu, R. J. Arner, C. C. Reddy, C. Krebs, and J. M. Bollinger, Jr.  Spectroscopic evidence for a coupled dinuclear iron cluster that coordinates the substrate in myo-inositol oxygenase.  Biochemistry 45:5393-5401.

Bollinger, J. M., Jr. and C. Krebs.  Stalking intermediates in oxygen activation by iron enzymes:  Motivation and method.  J. Inorg. Biochem. 100:586-605.

Behan, R. K., K. L. Stone, L. M. Hoffart, C. Krebs, and M. T. Green.  Evidence for protonated ferryls in compound II of cytochromes P450.  J. Am. Chem. Soc. 128:11471-11474.

Stone, K. L., L. M. Hoffart, R. K. Behan, C. Krebs, and M. T. Green.  Evidence for two ferryl species in chloroperoxidase compound II.  J. Am. Chem. Soc. 128:6147-6153.

Heinnickel, M., R. Agalarov, N. Svensen, C. Krebs, and J. H. Golbeck.  Identification of FX in the heliobacterial reaction center as a [4Fe-4S] cluster with an S = 3/2 ground spin state. Biochemistry 45:6756-6764.

2005

Bollinger, J. M. Jr., J. C. Price, L. M. Hoffart, E. W. Barr, and C. Krebs. Mechanism of taurine: a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Eur. J. Inorg. Chem. 21:4245-4254.

 
Smith, A. D., G. N. L. Jameson, P. C. Dos Santos, J. N. Agar, S. Naik, C. Krebs, J. Frazzon, D. R. Dean, B. H. Huynh, and M. K. Johnson. NifS-mediated assembly of [4Fe-4S] clusters in the N- and C-terminal domains of the NifU scaffold protein.  Biochemistry 44:12955-12969.
 
Price, J. C., E. W. Barr, L. M. Hoffart, C. Krebs, and J. M. Bollinger, Jr. Kinetic dissection of the catalytic mechanism of taurine: a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 44:8138-8147.
 
Cicchillo, R. M., L. Tu, J. A. Stromberg, L. M. Hoffart, C. Krebs, and S. J. Booker.  Escherichia coli quinolinate synthetase does indeed harbor a [4Fe-4S] cluster. J. Amer. Chem. Soc. 127:7310-7311.
 
Krebs, C., J. C. Price, J. Baldwin, L. Saleh, M. T. Green, and J. M. Bollinger, Jr. Rapid freeze-quench 57Fe-Mössbauer spectroscopy: Monitoring changes of an iron-containing active site during a biochemical reaction. Inorg. Chem. 44:742-757.

2004

Cicchillo, R.M., K.-H. Lee, C. Baleanu-Gogonea, N.M. Nesbitt, C. Krebs, and S.J. Booker. Escherichia coli lipoyl synthase binds two distinct [4Fe-4S] clusters per polypeptide. Biochemistry 43:11770-11781.

Cicchillo, R.M., M.A. Baker, E.J. Schnitzer, E.B. Newman, C. Krebs, and S.J. Booker. Escherichia coli L-serine deaminase requires a [4Fe-4S] cluster in catalysis. J. Biol. Chem. 279:32418-32425.

Riggs-Gelasco, P.J., J.C. Price, R.B. Guyer, J.H. Brehm, E.W. Barr, J.M. Bollinger, Jr., and C. Krebs. EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by Taurine:a-ketoglutarate dioxygenase. J. Am. Chem. Soc. 126:8108-8109.

Saleh, L., C. Krebs, B.A. Ley, S. Naik, B.H. Huynh, and J. Martin Bollinger, Jr. 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 43:5953-5964.

Mader Cosper, M., G.N.L. Jameson, H.L. Hernández, C. Krebs, B.H. Huynh, and M.K. Johnson. Characterization of the cofactor composition of Escherichia coli biotin synthase. Biochemistry 43:2007-2021.

Tripp, B.C., C.B. Bell III, F. Cruz, C. Krebs, and J.G. Ferry. A role for iron in an ancient carbonic anhydrase. J. Biol. Chem. 279:6683-6687.

2003

Price, J.C., E.W. Barr, T.E. Glass, C. Krebs, and J.M. Bollinger, Jr. Evidence for hydrogen abstraction from C1 of taurine by the high-spin Fe(IV) intermediate detected during oxygen activation by taurine:a-ketoglutarate dioxygenase (TauD). J. Am. Chem. Soc. 125:13008-13009.

Price, J.C., E.W. Barr, B. Tirupati, J.M. Bollinger, Jr. and C. Krebs. The first direct characterization of a high-valent iron intermediate in the reaction of an a-ketoglutarate-dependent dioxygenase: A high-spin Fe(IV) complex in taurine/a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42:7497-7508.

Hurshman, A.R., C. Krebs, D.E. Edmondson, and M.A. Marletta. Ability of tetrahydrobiopterin analogues to support catalysis by inducible nitric oxide synthase: Formation of a pterin radical is required for enzyme activity. Biochemistry 42:13287-13303.

Chaudhuri, P., E. Rentschler, F. Birkelbach, C. Krebs, E. Bill, T. Weyhermüller, and U. Flörke. Ground spin state variation in carboxylate-bridged tetranuclear [Fe₂Mn₂O₂]⁸⁺ cores and a comparison with their [Fe₄O₂]⁸⁺ and [Mn₄O₂]⁸⁺ congeners. Eur. J. Inorg. Chem. 2003:541-555.

Baldwin, J., C. Krebs, L. Saleh, M. Stelling, B.H. Huynh, J.M. Bollinger, Jr. and P.J. Riggs-Gelasco. 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 42:13269-13279.

Broderick, J.B., C. Walsby, W.E. Broderick, C. Krebs, W. Hong, D. Ortillo, J. Cheek, B.H. Huynh, and B.M. Hoffman. Paramagnetic resonance in mechanistic studies of Fe-S/radical enzymes. In: Paramagnetic Resonance of Metallobiomolecules. (J. Telser, ed.), pp 113-127, American Chemical Society, Washington, D. C.

2002

Krebs, C., W.E. Broderick, T.F. Henshaw, J.B. Broderick, and B.H. Huynh. Coordination of adenosylmethionine to a unique iron site of the [4Fe-4S] of pyruvate formate-lyase activating enzyme: A Mössbauer spectroscopic study. J. Am. Chem. Soc. 124:912-913.

Yun, D., C. Krebs, G.P. Gupta, D.F. Iwig, B.H. Huynh, and J.M Bollinger, Jr. 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. 41:981-990.

Lee, D., B. Pierce, C. Krebs, M.P. Hendrich, B.H. Huynh, and S.J. Lippard. 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. J. Am. Chem. Soc. 124:3993-4007.

Krebs, C., J.M. Bollinger, Jr., E.C. Theil, and B.H. Huynh. Exchange coupling constant J of peroxodiferric reaction intermediates determined by Mössbauer spectroscopy. J. Biol. Inorg. Chem. 7:863-869.

Krebs, C., D.E. Edmondson, and B.H. Huynh. Demonstration of peroxodiferric intermediate in M-ferritin ferroxidase reaction using rapid freeze-quench Mössbauer, resonance raman, and XAS spectroscopies. Methods Enzymol. 354:436-454.

Lee, D., B. Pierce, C. Krebs, M.P. Hendrich, B.H. Huynh, and S.J. Lippard. 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. J. Am. Chem. Soc. 124:3993-4007.