1993
DOI: 10.1073/pnas.90.6.2179
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Cytochromes c biogenesis in a photosynthetic bacterium requires a periplasmic thioredoxin-like protein.

Abstract: Rhodobacter capsulatus is a

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Cited by 107 publications
(121 citation statements)
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References 41 publications
(33 reference statements)
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“…2, as are representative genera that possess each system. For systems I and II, there is a good understanding of how the CXXCH cysteines are reduced, using a general transmembrane thioredox protein such as DsbD (101) (or the smaller, related CcdA [43,139]) and dedicated thioredoxins such as CcsX (23) or CcmG (24). Figure 2 diagrams the thiol proteins (in red) which transfer reducing equivalents from inside the cell to outside.…”
Section: Cytochrome C Biogenesis: Three Systems and Some Emerging Spmentioning
confidence: 99%
“…2, as are representative genera that possess each system. For systems I and II, there is a good understanding of how the CXXCH cysteines are reduced, using a general transmembrane thioredox protein such as DsbD (101) (or the smaller, related CcdA [43,139]) and dedicated thioredoxins such as CcsX (23) or CcmG (24). Figure 2 diagrams the thiol proteins (in red) which transfer reducing equivalents from inside the cell to outside.…”
Section: Cytochrome C Biogenesis: Three Systems and Some Emerging Spmentioning
confidence: 99%
“…However, by analogy with Rhodobacter capszrlatus and Bra4rhixobizrm japonicum, we would expect at least nine genes to be essential for the synthesis of cytochrome cL in addition to its structural gene, mxaG (Ramseier e t al., 1991;Beckman e t al., 1992;Ritz et al, 1993;Beckman & Kranz, 1993;Thonymeyer e t al., 1994a, b).…”
Section: Production Of Cytochrome Cmentioning
confidence: 99%
“…The haem-binding site (Cys-X-XCys-His) of the cytochrome c must be reduced before haem attachment can take place and a thioredoxin-like protein is probably required for this (Beckman & Kranz, 1993 ; Thonymeyer e t al.,…”
mentioning
confidence: 99%
“…A plausible current model is that the two cysteine residues in the CXXCH motif of a polypeptide destined to become a c-type cytochrome are oxidized to a disulfide bridge before re-reduction linked to the attachment of the haem (Metheringham et al, 1995 ;Sambongi & Ferguson, 1996). This re-reduction is proposed to involve DipZ, either directly or as a donor of reducing power to a periplasmic thioredoxin-like protein, CcmG (Sambongi & Ferguson, 1994;, which is specifically required for periplasmic c-type cytochrome biogenesis (Beckman & Kranz, 1993;Thony-Meyer et al, 1995). Whereas the first E. coli mutant found to be pleiotropically deficient in c-type cytochromes was mutated in d i p z , it is very striking that this gene has never been found in screens for c-type cytochrome deficiency in several other organisms including Rhodobacter capsulatus, Paracoccus denitrificans and Bradyrhizobium japonicum.…”
Section: D Page N F W S a U N D E R S A N D S J F E R G U mentioning
confidence: 99%