Abstract: Abstract Nine heme cytochrome c (9Hcc) is a monomeric multi‐heme cytochrome c found in the sulfate‐reducing bacteria of Desulfovibrio desulfuricans (Dd) ATCC 27774 and Desulfovibrio desulfuricans Essex 6. The polypeptide chain comprises 296 residues and wraps around nine hemes of type‐c that bind the polypeptide chain through thioether bridges to cysteine residues. This represents the first known structure of a multi‐heme cytochrome where copies of a tetra‐heme cytochrome c 3 ‐like fold are present in the same polypeptide chain. The high homology between 9Hcc and the C‐terminal region of Desulfovibrio vulgaris Hildenborough (DvH) Hmc, as well as the presence of the 9Hcc gene within an operon similar to that of the DvH Hmc, strongly support the proposal that 9Hcc is the high‐molecular‐weight cytochrome of Dd. Several in vitro studies, as well as our crystallographic and modeling studies suggest that cytochrome c 3 is the mediator between the [NiFe] hydrogenase and 9Hcc in Dd.
Publication Year: 2004
Publication Date: 2004-03-05
Language: en
Type: other
Indexed In: ['crossref']
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Cited By Count: 1
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