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- W1569250885 abstract "Hydrogenophilus thermoluteolus cytochrome c ′ (PHCP) has typical spectral properties previously observed for other cytochromes c ′, which comprise Ambler’s class II cytochromes c . The PHCP protein sequence (135 amino acids) deduced from the cloned gene is the most homologous (55% identity) to that of cytochrome c ′ from Allochromatium vinosum (AVCP). These findings indicate that PHCP forms a four‐helix bundle structure, similar to AVCP. Strikingly, PHCP with a covalently bound heme was heterologously synthesized in the periplasm of Escherichia coli strains deficient in the DsbD protein, a component of the System I cytochrome c biogenesis machinery. The heterologous synthesis of PHCP by aerobically growing E. coli also occurred without a plasmid carrying the genes for Ccm proteins, other components of the System I machinery. Unlike Ambler’s class I general cytochromes c , the synthesis of PHCP is not dependent on the System I machinery and exhibits similarity to that of E. coli periplasmic cytochrome b 562 , a 106‐residue four‐helix bundle. Database The sequence data reported here have been deposited in the DDBJ database under accession no. AB617519 ." @default.
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- W1569250885 date "2011-05-25" @default.
- W1569250885 modified "2023-10-18" @default.
- W1569250885 title "Heterologous synthesis of cytochrome c′ by Escherichia coli is not dependent on the System I cytochrome c biogenesis machinery" @default.
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- W1569250885 doi "https://doi.org/10.1111/j.1742-4658.2011.08155.x" @default.
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