Journal of Molecular Medicine

, Volume 78, Issue 5, pp 239–242

Cytochrome c oxidase assembly factors with a thioredoxin fold are conserved among prokaryotes and eukaryotes

  • Yurii V. Chinenov
Bioinformatics

DOI: 10.1007/s001090000110

Cite this article as:
Chinenov, Y. J Mol Med (2000) 78: 239. doi:10.1007/s001090000110

Abstract.

Cytochrome c oxidase (COX) is a multi-subunit terminal oxidase of the eukaryotic respiratory chain involved in the reduction of oxygen to water. Numerous lines of evidence suggest that the assembly of COX is a multi-step, assisted process that depends on several assembly factors with largely unknown functions. Sco1/2 proteins have been isolated as high-copy number suppressors of a deletion of copper chaperone Cox17, implicating Sco1/2 in copper transport to COX subunits I or II. Here I report the similarity of Sco1/2 assembly factors to peroxiredoxins and thiol:disulfide oxidoreductases with a thioredoxin fold, suggesting that Sco-related proteins perform a catalytic rather than a copper transport function. Reported sequence similarities, together with the functional role of bacterial Sco-related proteins suggest that Sco-related proteins represent a new class of membrane-anchored thiol:disulfide oxidoreductases involved in COX maturation.

Sco Cytochrome c oxidase Peroxiredoxins Thioredoxin fold Cox17

Copyright information

© Springer-Verlag 2000

Authors and Affiliations

  • Yurii V. Chinenov
    • 1
  1. 1.Howard Hughes Medical Institute, University of Michigan Medical Center, 4570 MSRB II, 1150 W. Medical Center Drive, Ann Arbor, MI 48109-0650USA