Journal Home
Search for

Volume 580, Issue 9, Pages 2166-2169 (17 April 2006)


View previous. 4 of 41 View next.

Cytochrome c6A is a funnel for thiol oxidation in the thylakoid lumen

Edited by Richard Cogdell

Beatrix G. Schlarb-Ridleya, Robert H. Nimmoa, Saul Purtonb, Christopher J. HoweaCorresponding Author Informationemail address, Derek S. Bendalla

Received 2 March 2006; received in revised form 17 March 2006; accepted 20 March 2006. published online 27 March 2006.

Abstract 

Cytochrome c6A is a dithio-cytochrome recently discovered in land plants and green algae, and believed to be derived from the well-known cytochrome c6. The function of cytochrome c6A is unclear. We propose that it catalyses the formation of disulphide bridges in thylakoid lumen proteins in a single-step disulphide exchange reaction, with subsequent transfer of the reducing equivalents to plastocyanin. The haem group of cytochrome c6A acts as an electron sink, allowing rapid resolution of a radical intermediate formed during reoxidation of cytochrome c6A. Our model is consistent with previously published data on mutant plants, and the likely evolution of the protein.

a Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK

b Department of Biology, University College London, London WC1E 6BT, United Kingdom

Corresponding Author InformationCorresponding author. Fax: +44 1223 333345.

PII: S0014-5793(06)00367-X

doi:10.1016/j.febslet.2006.03.052


View previous. 4 of 41 View next.