Krebs C - Search Results

1

A New Microbial Pathway for Organophosphonate Degradation Catalyzed by Two Previously Misannotated Non-Heme-Iron Oxygenases.

Rajakovich LJ, Pandelia ME, Mitchell AJ, Chang WC, Zhang B, Boal AK, Krebs C, Bollinger JM Jr. Rajakovich LJ, et al. Among authors: krebs c. Biochemistry. 2019 Mar 26;58(12):1627-1647. doi: 10.1021/acs.biochem.9b00044. Epub 2019 Mar 7. Biochemistry. 2019. PMID: 30789718 Free PMC article.

2

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.

Yun D, Krebs C, Gupta GP, Iwig DF, Huynh BH, Bollinger JM Jr. Yun D, et al. Among authors: krebs c. Biochemistry. 2002 Jan 22;41(3):981-90. doi: 10.1021/bi011797p. Biochemistry. 2002. PMID: 11790122

3

Exchange coupling constant J of peroxodiferric reaction intermediates determined by Mössbauer spectroscopy.

Krebs C, Bollinger JM Jr, Theil EC, Huynh BH. Krebs C, et al. J Biol Inorg Chem. 2002 Sep;7(7-8):863-9. doi: 10.1007/s00775-002-0371-1. Epub 2002 Apr 27. J Biol Inorg Chem. 2002. PMID: 12203023

4

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.

Price JC, Barr EW, Tirupati B, Bollinger JM Jr, Krebs C. Price JC, et al. Among authors: krebs c. Biochemistry. 2003 Jun 24;42(24):7497-508. doi: 10.1021/bi030011f. Biochemistry. 2003. PMID: 12809506

5

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).

Price JC, Barr EW, Glass TE, Krebs C, Bollinger JM Jr. Price JC, et al. Among authors: krebs c. J Am Chem Soc. 2003 Oct 29;125(43):13008-9. doi: 10.1021/ja037400h. J Am Chem Soc. 2003. PMID: 14570457

6

Structural characterization of the peroxodiiron(III) intermediate generated during oxygen activation by the W48A/D84E variant of ribonucleotide reductase protein R2 from Escherichia coli.

Baldwin J, Krebs C, Saleh L, Stelling M, Huynh BH, Bollinger JM Jr, Riggs-Gelasco P. Baldwin J, et al. Among authors: krebs c. Biochemistry. 2003 Nov 18;42(45):13269-79. doi: 10.1021/bi035198p. Biochemistry. 2003. PMID: 14609338

7

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.

Saleh L, Krebs C, Ley BA, Naik S, Huynh BH, Bollinger JM Jr. Saleh L, et al. Among authors: krebs c. Biochemistry. 2004 May 25;43(20):5953-64. doi: 10.1021/bi036099e. Biochemistry. 2004. PMID: 15147179

8

EXAFS spectroscopic evidence for an Fe=O unit in the Fe(IV) intermediate observed during oxygen activation by taurine:alpha-ketoglutarate dioxygenase.

Riggs-Gelasco PJ, Price JC, Guyer RB, Brehm JH, Barr EW, Bollinger JM Jr, Krebs C. Riggs-Gelasco PJ, et al. Among authors: krebs c. J Am Chem Soc. 2004 Jul 7;126(26):8108-9. doi: 10.1021/ja048255q. J Am Chem Soc. 2004. PMID: 15225039

9

Rapid freeze-quench 57Fe Mössbauer spectroscopy: monitoring changes of an iron-containing active site during a biochemical reaction.

Krebs C, Price JC, Baldwin J, Saleh L, Green MT, Bollinger JM Jr. Krebs C, et al. Inorg Chem. 2005 Feb 21;44(4):742-57. doi: 10.1021/ic048523l. Inorg Chem. 2005. PMID: 15859243

10

Kinetic dissection of the catalytic mechanism of taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli.

Price JC, Barr EW, Hoffart LM, Krebs C, Bollinger JM Jr. Price JC, et al. Among authors: krebs c. Biochemistry. 2005 Jun 7;44(22):8138-47. doi: 10.1021/bi050227c. Biochemistry. 2005. PMID: 15924433

Recent studies on taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli have provided evidence for a three-step, minimal kinetic mechanism involving the quaternary TauD.Fe(II).alpha-ketoglutarate.taurine complex, the taurine-hydroxylating Fe(IV)-oxo intermediate (J …

Recent studies on taurine:alpha-ketoglutarate dioxygenase (TauD) from Escherichia coli have provided evidence for a three-step, minimal kine …

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