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The tetraheme cytochrome CymA is required for anaerobic respiration with dimethyl sulfoxide and nitrite in Shewanella oneidensis.
It is shown here, by direct measurements of electron transfer between the purified proteins, that CymA(sol) efficiently reduces S. oneidensis fumarate reductase, indicating that no further proteins are required for electrontransfer between the quinone pool and fumidate if the authors assume direct reduction of Cym a by quinols. Expand
Roles of key active-site residues in flavocytochrome P450 BM3.
Mutants F87G and F87Y not only exhibit increased Km and decreased kcat values for fatty acid oxidation, but also undergo an irreversible conversion process from a 'fast' to a 'slow' rate of substrate turnover. Expand
The membrane-bound tetrahaem c-type cytochrome CymA interacts directly with the soluble fumarate reductase in Shewanella.
The expression, purification and characterization of a soluble, truncated CymA, a member of the NapC/NirT family, is described, suggesting that 'CymA is an efficient electron donor for the soluble fumarate reductase, flavocytochrome c(3). Expand
Expression, purification, and characterization of Bacillus subtilis cytochromes P450 CYP102A2 and CYP102A3: flavocytochrome homologues of P450 BM3 from Bacillus megaterium.
Comparison of the amino acid sequences of the three flavocytochromes shows that several important amino acids in P450 BM3 are not conserved in the B. subtilis homologues, pointing to differences in the binding modes for the substrates that may explain the unusual sigmoidal kinetic and titration properties. Expand
P450 BM3: the very model of a modern flavocytochrome.
The fundamental properties of P 450 BM3 are discussed and how progress with this model P450 has affected the authors' comprehension of P450 systems in general is discussed. Expand
Molecular insights into substrate recognition and catalysis by tryptophan 2,3-dioxygenase
- F. Forouhar, J. Anderson, +14 authors L. Tong
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences
- 9 January 2007
Tryptophan 2,3-dioxygenase (TDO) and indoleamine 2,3-dioxygenase (IDO) constitute an important, yet relatively poorly understood, family of heme-containing enzymes. Here, we report extensive… Expand
Sequence of the gene encoding flavocytochrome c from Shewanella putrefaciens: a tetraheme flavoenzyme that is a soluble fumarate reductase related to the membrane-bound enzymes from other bacteria.
- S. L. Pealing, A. Black, F. Manson, F. B. Ward, S. Chapman, G. Reid
- Chemistry, Medicine
- 8 December 1992
The sequence of the flavoprotein domain demonstrates an even closer relationship with the product of the yeast OSM1 gene, mutations in which result in sensitivity to high osmolarity. Expand
Exploring the mechanism of tryptophan 2,3-dioxygenase
- Sarah J. Thackray, C. Mowat, S. Chapman
- Chemistry, Medicine
- Biochemical Society transactions
- 19 November 2008
The function, structure and possible catalytic mechanism of TDO and IDO are discussed and the mechanisms employed by these enzymes in the binding and activation of dioxygen and tryptophan are discussed. Expand
Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration.
- E. Gordon, A. Pike, A. E. Hill, P. M. Cuthbertson, S. Chapman, G. Reid
- The Biochemical journal
A null mutant by gene disruption is constructed and Shewanella frigidimarina lacking cytochrome c(3) grows well aerobically and its growth rate under anaerobiosis with a variety of electron acceptors is indistinguishable from that of the wild-type parent strain, except that respiration with Fe(III) as sole acceptor is severely, although not completely, impaired. Expand
Determination of the redox properties of human NADPH-cytochrome P450 reductase.
The redox properties of human cytochrome P450 reductase (CPR) are similar to those reported for rabbit CPR and the reduct enzyme domain of neuronal nitric oxide synthase, however, they differ markedly from those of yeast and bacterial CPRs, pointing to an important evolutionary difference in electronic regulation of these enzymes. Expand