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The "b5-like" domain from chicken-liver sulfite oxidase: a new case of common ancestral origin with liver cytochrome b5 and bakers' yeast cytochrome b2 core.
Guiard B, Lederer F. Guiard B, et al. Among authors: lederer f. Eur J Biochem. 1977 Mar 15;74(1):181-90. doi: 10.1111/j.1432-1033.1977.tb11379.x. Eur J Biochem. 1977. PMID: 404144
Crystal structure analysis of recombinant rat kidney long chain hydroxy acid oxidase.
Cunane LM, Barton JD, Chen ZW, Lê KH, Amar D, Lederer F, Mathews FS. Cunane LM, et al. Among authors: lederer f. Biochemistry. 2005 Feb 8;44(5):1521-31. doi: 10.1021/bi048616e. Biochemistry. 2005. PMID: 15683236
Flavocytochrome b2: reactivity of its flavin with molecular oxygen.
Boubacar AK, Pethe S, Mahy JP, Lederer F. Boubacar AK, et al. Among authors: lederer f. Biochemistry. 2007 Nov 13;46(45):13080-8. doi: 10.1021/bi7013757. Epub 2007 Oct 23. Biochemistry. 2007. PMID: 17956127
Probing intramolecular electron transfer within flavocytochrome b2 with a monoclonal antibody.
Miles CS, Lederer F, Lê KH. Miles CS, et al. Among authors: lederer f. Biochemistry. 1998 Mar 10;37(10):3440-8. doi: 10.1021/bi972639u. Biochemistry. 1998. PMID: 9521665
Crystallographic study of bakers' yeast cytochrome b2.
Mathews FS, Lederer F. Mathews FS, et al. Among authors: lederer f. J Mol Biol. 1976 Apr 25;102(4):853-7. doi: 10.1016/0022-2836(76)90295-3. J Mol Biol. 1976. PMID: 781266 No abstract available.
Potentiometric and further kinetic characterization of the flavin-binding domain of Saccharomyces cerevisiae flavocytochrome b2. Inhibition by anions binding in the active site.
Cénas N, Lê KH, Terrier M, Lederer F. Cénas N, et al. Among authors: lederer f. Biochemistry. 2007 Apr 17;46(15):4661-70. doi: 10.1021/bi602634y. Epub 2007 Mar 21. Biochemistry. 2007. PMID: 17373777
Kinetic and crystallographic studies on the active site Arg289Lys mutant of flavocytochrome b2 (yeast L-lactate dehydrogenase).
Mowat CG, Beaudoin I, Durley RC, Barton JD, Pike AD, Chen ZW, Reid GA, Chapman SK, Mathews FS, Lederer F. Mowat CG, et al. Among authors: lederer f. Biochemistry. 2000 Mar 28;39(12):3266-75. doi: 10.1021/bi9925975. Biochemistry. 2000. PMID: 10727218
Baker's yeast flavocytochrome b2. A mechanistic study of the dehydrohalogenation reaction.
Urban P, Lederer F. Urban P, et al. Among authors: lederer f. Eur J Biochem. 1984 Oct 15;144(2):345-51. doi: 10.1111/j.1432-1033.1984.tb08470.x. Eur J Biochem. 1984. PMID: 6386468
It has been shown that reduced flavocytochrome b2 not only catalyzes reduction of bromopyruvate [P. Urban, P.M. Alliel and F. Lederer (1983) Eur. J. Biochem. 134, 275-281] but also transforms it into pyruvate in a reductive elimination process. ...
It has been shown that reduced flavocytochrome b2 not only catalyzes reduction of bromopyruvate [P. Urban, P.M. Alliel and F. Lede
Methionyl-tRNA synthetase from Escherichia coli: primary structure at the binding site for the 3'-end of tRNAfMet.
Hountondji C, Blanquet S, Lederer F. Hountondji C, et al. Among authors: lederer f. Biochemistry. 1985 Feb 26;24(5):1175-80. doi: 10.1021/bi00326a018. Biochemistry. 1985. PMID: 3913464
Inactivation of flavocytochrome b2 with fluoropyruvate. Reaction at the active-site histidine.
Urban P, Lederer F. Urban P, et al. Among authors: lederer f. Eur J Biochem. 1988 Apr 5;173(1):155-62. doi: 10.1111/j.1432-1033.1988.tb13979.x. Eur J Biochem. 1988. PMID: 3356187
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