Continued surprises in the cytochrome c biogenesis story.


Sawyer, EB; Barker, PD; (2012) Continued surprises in the cytochrome c biogenesis story. Protein & cell, 3 (6). pp. 405-9. ISSN 1674-800X DOI: https://doi.org/10.1007/s13238-012-2912-x

Full text not available from this repository. (Request a copy)

Abstract

Cytochromes c covalently bind their heme prosthetic groups through thioether bonds between the vinyl groups of the heme and the thiols of a CXXCH motif within the protein. In Gram-negative bacteria, this process is catalyzed by the Ccm (cytochrome c maturation) proteins, also called System I. The Ccm proteins are found in the bacterial inner membrane, but some (CcmE, CcmG, CcmH, and CcmI) also have soluble functional domains on the periplasmic face of the membrane. Elucidation of the mechanisms involved in the transport and relay of heme and the apocytochrome from the bacterial cytosol into the periplasm, and their subsequent reaction, has proved challenging due to the fact that most of the proteins involved are membrane-associated, but recent progress in understanding some key components has thrown up some surprises. In this Review, we discuss advances in our understanding of this process arising from a substrate's point of view and from recent structural information about individual components.

Item Type: Article
Faculty and Department: Faculty of Infectious and Tropical Diseases > Dept of Pathogen Molecular Biology
PubMed ID: 22723177
URI: http://researchonline.lshtm.ac.uk/id/eprint/4645903

Statistics


Download activity - last 12 months
Downloads since deposit
0Downloads
4Hits
Accesses by country - last 12 months
Accesses by referrer - last 12 months
Impact and interest
Additional statistics for this record are available via IRStats2

Actions (login required)

Edit Item Edit Item