Journal
TRENDS IN MICROBIOLOGY
Volume 18, Issue 6, Pages 266-274Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.tim.2010.03.006
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Funding
- Department of Energy [91ER 20052]
- National Institutes of Health [GM 38237]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM038237] Funding Source: NIH RePORTER
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Cytochromes of c-type contain covalently attached hemes that are formed via thioether bonds between the vinyls of heme b and cysteines within C1XXC2H motifs of apocytochromes. In diverse organisms this post-translational modification relies on membrane-associated specific biogenesis proteins, referred to as cytochrome c maturation (Ccm) systems. A highly complex version of these systems, Ccm or System I, is found in Gram-negative bacteria, archaea and plant mitochondria. We describe emerging functional interactions between the Ccm components categorized into three conserved modules, and present a mechanistic view of the molecular basis of ubiquitous vinyl-2 similar to Cys(1) and vinyl-4 similar to Cys(2) heme b-apocytochrome thioether bonds in c-type cytochromes.
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