Copper trafficking to the mitochondrion and assembly of copper metalloenzymes

被引：242
作者：
Cobine, Paul A.
Pierrel, Fabien
Winge, Dennis R. [1 ]
机构：
[1] Univ Utah, Hlth Sci Ctr, Dept Med, Salt Lake City, UT 84132 USA
[2] Univ Utah, Hlth Sci Ctr, Dept Biochem, Salt Lake City, UT 84132 USA
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2006年 / 1763卷 / 07期
关键词：
copper; mitochondrion; cytochrome oxidase; metallochaperone;
D O I：
10.1016/j.bbamcr.2006.03.002
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Copper is required within the mitochondrion for the function of two metalloenzymes, cytochrome c oxidase (CcO) and superoxide dismutase (Sod1). Copper metallation of these two enzymes occurs within the mitochondrial intermembrane space and is mediated by metallochaperone proteins. Cox17 is a key copper donor to two accessory proteins, Sco1 and Cox11, to form the two copper centers in the mature CcO complex. Ccs1 is the necessary metallochaperone for the copper metallation of Sod1 in the IMS as well as within the cytoplasm where the. bulk of Sod1 resides. Copper ions used in the metallation of CcO and Sod1 appear to be provided by a novel copper pool within the mitochondrial matrix. This review documents copper ion shuttling within the mitochondrion and the proteins that mediate assembly of active CcO and Sod1. (c) 2006 Elsevier B.V. All rights reserved.
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收藏
页码：759 / 772
页数：14
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