Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.

Original publication

DOI

10.1016/j.bbabio.2008.03.020

Type

Journal article

Journal

Biochim Biophys Acta

Publication Date

07/2008

Volume

1777

Pages

980 - 984

Keywords

Amino Acid Sequence, Cysteine, Cytochromes c, Electron Transport, Genetic Variation, Humans, Lyases, Mitochondria, Protein Processing, Post-Translational, Sulfides