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EcoSal Plus

Domain 3:

Metabolism

Cytochrome Biogenesis

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  • Authors: Julie M. Stevens1, and Stuart J. Ferguson2
  • Editor: Tadhg P. Begley3
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Department of Biochemistry, University of Oxford, Oxford, United Kingdom; 2: Department of Biochemistry, University of Oxford, Oxford, United Kingdom; 3: Texas A&M University, College Station, Texas
  • Received 27 February 2008 Accepted 05 May 2008 Published 07 November 2008
  • Address correspondence to Julie M. Stevens julie.stevens@bioch.ox.ac.uk
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  • Abstract:

    employs several -type cytochromes, which are found in the periplasm or on the periplasmic side of the cytoplasmic membrane; they are used for respiration under different growth conditions. All -type cytochromes are multiheme cytochromes; does not have a monoheme cytochrome of the kind found in mitochondria. The attachment of heme to cytochromes occurs in the periplasm, and so the apoprotein must be transported across the cytoplasmic membrane; this step is mediated by the Sec system, which transports unfolded proteins across the membrane. The protein CcmE has been found to bind heme covalently via a single bond and then transfer the heme to apocytochromes. It should be mentioned that far less complex systems for cytochrome biogenesis exist in other organisms and that enterobacteria do not function as a representative model system for the process in general, although plant mitochondria use the Ccm system found in . The variety and distribution of cytochromes and their biogenesis systems reflect their significance and centrality in cellular bioenergetics, though the necessity for and origin of the diverse biogenesis systems are enigmatic.

  • Citation: Stevens J, Ferguson S. 2008. Cytochrome Biogenesis, EcoSal Plus 2008; doi:10.1128/ecosalplus.3.6.3.12

References

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/content/journal/ecosalplus/10.1128/ecosalplus.3.6.3.12
2008-11-07
2017-05-29

Abstract:

employs several -type cytochromes, which are found in the periplasm or on the periplasmic side of the cytoplasmic membrane; they are used for respiration under different growth conditions. All -type cytochromes are multiheme cytochromes; does not have a monoheme cytochrome of the kind found in mitochondria. The attachment of heme to cytochromes occurs in the periplasm, and so the apoprotein must be transported across the cytoplasmic membrane; this step is mediated by the Sec system, which transports unfolded proteins across the membrane. The protein CcmE has been found to bind heme covalently via a single bond and then transfer the heme to apocytochromes. It should be mentioned that far less complex systems for cytochrome biogenesis exist in other organisms and that enterobacteria do not function as a representative model system for the process in general, although plant mitochondria use the Ccm system found in . The variety and distribution of cytochromes and their biogenesis systems reflect their significance and centrality in cellular bioenergetics, though the necessity for and origin of the diverse biogenesis systems are enigmatic.

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Figure 1

Citation: Stevens J, Ferguson S. 2008. Cytochrome Biogenesis, EcoSal Plus 2008; doi:10.1128/ecosalplus.3.6.3.12
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Image of Figure 2
Figure 2

The cysteine residues in the thiol oxidoreductases are shown in yellow; there is a conserved pair of cysteines in the transmembrane domain of DsbD that are involved in the disulfide cascade. The identity of the transported substrate of CcmAB (and whether there is one) is unknown. The heme-binding histidine of CcmE is shown in blue. CcmC facilitates heme provision to CcmE, and CcmF is thought to facilitate heme release and transfer to the apocytochrome. DsbA oxidizes the apocytochrome, which is subsequently reversed by an electron flow from DsbD via CcmG. DsbB transfers electrons from DsbA to ubiquinone in the membrane. It is not known how heme is exported from its cytoplasmic site of synthesis. The structures shown, which are from unless otherwise indicated, are from the Protein Data Bank entries for the following proteins and domains: CcmE (1SR3) ( 7 ), CcmH (from ; 2E2E) ( 8 ), CcmG (1KNG) ( 9 ), the N-terminal domain of DsbD (1I6P) ( 10 ), the C-terminal domain of DsbD (1UC7) ( 11 ), TrxA (thioredoxin; 2TRX) ( 12 ), and DsbAB (2H17) ( 13 ). The cytochrome shown is cytochrome from (155C) ( 14 ). The structures were rendered in PyMOL (W. L. DeLano, The PyMOL Molecular Graphics System, 2002; http://www.pymol.org).

Citation: Stevens J, Ferguson S. 2008. Cytochrome Biogenesis, EcoSal Plus 2008; doi:10.1128/ecosalplus.3.6.3.12
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