Cytochrome c assembly: a tale of ever increasing variation and mystery?
Formation of cytochromes c requires a deceptively simple post-translational modification, the formation of two thioether bonds (or rarely one) between the thiol groups of two cysteine residues found in a CXXCH motif (with some occasional variations) and the vinyl groups of heme. There are three partially characterised systems for facilitating this post-translational modification; within these systems there is also variation. In addition, there are clear indications for two other distinct systems. Here some of the current issues in understanding the systems are analysed.
Ferguson
Stuart J
SJ
Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. stuart.ferguson@bioch.ox.ac.uk
Stevens
Julie M
JM
Allen
James W A
JW
Robertson
Ian B
IB
D000595:Amino Acid Sequence; D003545:Cysteine / Q000378:metabolism; D045304:Cytochromes c / Q000235:genetics* / Q000378:metabolism*; D004579:Electron Transport; D014644:Genetic Variation; D006801:Humans; D008190:Lyases / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D013440:Sulfides / Q000378:metabolism
D013440:Sulfides; D045304:Cytochromes c; D008190:Lyases; D003545:Cysteine