Ontology highlight
ABSTRACT:
SUBMITTER: Mavridou DA
PROVIDER: S-EPMC3268396 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Mavridou Despoina A I DA Stevens Julie M JM Mönkemeyer Leonie L Daltrop Oliver O di Gleria Katalin K Kessler Benedikt M BM Ferguson Stuart J SJ Allen James W A JW
The Journal of biological chemistry 20111125 4
c-Type cytochromes are widespread proteins, fundamental for respiration or photosynthesis in most cells. They contain heme covalently bound to protein in a highly conserved, highly stereospecific post-translational modification. In many bacteria, mitochondria, and archaea this heme attachment is catalyzed by the cytochrome c maturation (Ccm) proteins. Here we identify and characterize a covalent, ternary complex between the heme chaperone CcmE, heme, and cytochrome c. Formation of the complex fr ...[more]