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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
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.
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
Import of cytochrome b2 to the mitochondrial intermembrane space: The tightly folded heme‐binding domain makes import dependent upon matrix ATP
Results indicate that cytochrome b2 reaches the intermembrane space without completely crossing the inner membrane, and some precursors fold outside the mitochondria but remain translocation‐competent, and import of these precursor in vitro does not require ATP‐dependent cytosolic chaperone proteins. Expand
Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration.
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
Rational re‐design of the substrate binding site of flavocytochrome P450 BM3
Removing the arginine 47/lysine 51 carboxylate binding motif at the mouth of the active site disfavours binding of all fatty acids, indicating its importance in the initial recognition of substrates. Expand
Expression, purification and spectroscopic characterization of the cytochrome P450 CYP121 from Mycobacterium tuberculosis.
The CYP121 gene from the pathogenic bacterium Mycobacterium tuberculosis has been cloned and expressed in Escherichia coli, and the protein purified to homogeneity by ion exchange and hydrophobic interaction chromatography suggests that it may represent a novel target for these antibiotics in the M. tuberculosis pathogen. Expand
Characterization of a flavocytochrome that is induced during the anaerobic respiration of Fe3+ by Shewanella frigidimarina NCIMB400.
A 63.9 kDa periplasmic tetrahaem flavocytochrome c(3), designated Ifc(3), was found to be expressed in Shewanella frigidimarina NCIMB400 grown anaerobically with ferric citrate or ferricExpand
Structural and mechanistic mapping of a unique fumarate reductase
The 1.8 Å resolution crystal structure of the tetraheme flavocytochrome c3, Fcc3, provides the first mechanistic insight into respiratory fumarate reductases or succinate dehydrogenases. TheExpand