Characterization of the copper chaperone Cox17 of Saccharomyces cerevisiae

被引：96
作者：
Srinivasan, C
Posewitz, MC
George, GN
Winge, DR [1 ]
机构：
[1] Univ Utah, Hlth Sci Ctr, Salt Lake City, UT 84132 USA
[2] Stanford Univ, Stanford Linear Accelerator Ctr, Stanford Synchrotron Radiat Lab, Stanford, CA 94309 USA
来源：
BIOCHEMISTRY | 1998年 / 37卷 / 20期
关键词：
D O I：
10.1021/bi980418y
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：
Assembly of functional cytochrome oxidase in yeast requires Cox17, which has been postulated to deliver copper ions to the mitochondrion for insertion into the enzyme. This role for Cox17 is supported by the observation that it binds copper as a binuclear cuprous-thiolate cluster. X-ray absorption spectroscopy, together with UV-visible absorption and emission spectroscopy, indicates the presence of bound cuprous ions, trigonally coordinated by thiolate ligands. Analysis of the EXAFS shows three Cu-S bonds at 2.26 Angstrom, plus a short Cu-Cu distance of 2.7 Angstrom, indicating a binuclear cluster in Cox17. The cuprous-thiolate cluster in Cox17 is substantially more labile than structurally related clusters in metallothioneins.
引用
收藏
页码：7572 / 7577
页数：6
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