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 membraneassociated 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~ys1 and vinyl-4~ys2 heme b-apocytochrome thioether bonds in c-type cytochromes.
Bibliographical noteFunding Information:
This work is supported by grants to F.D. from the Department of Energy (91ER 20052) and the National Institutes of Health (GM 38237).
All Science Journal Classification (ASJC) codes
- Microbiology (medical)
- Infectious Diseases