Function and redox state of mitochondrial localized cysteine-rich proteins important in the assembly of cytochrome c oxidase

Authors

Oleh Khalimonchuk, University of Nebraska-LincolnFollow
Dennis R. Winge, University of Utah Health Sciences Center

Document Type

Article

Date of this Version

2008

Citation

Biochim Biophys Acta. 2008 April ; 1783(4): 618–628.

Comments

Copyright 2008 Elsevier. Used by permission.

Abstract

The cytochrome c oxidase (CcO) complex of the mitochondrial respiratory chain exists within the mitochondrial inner membrane (IM). The biogenesis of the complex is a multi-faceted process requiring multiple assembly factors that function on both faces of the IM. Formation of the two copper centers of CcO occurs within the intermembrane space (IMS) and is dependent on assembly factors with critical cysteinyl thiolates. Two classes of assembly factors exist, one group being soluble IMS proteins and the second class being proteins tethered to the IM. A common motif in the soluble assembly factors is a duplicated Cx₉C sequence motif. Since mitochondrial respiration is a major source of reactive oxygen species, control of the redox state of mitochondrial proteins is an important process. This review documents the role of these cysteinyl CcO assembly factors within the IMS and the necessity of redox control in their function.