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J. Biol. Chem., Vol. 281, Issue 48, 36552-36559, December 1, 2006

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Mitochondrial Matrix Copper Complex Used in Metallation of Cytochrome Oxidase and Superoxide Dismutase^*

From the University of Utah Health Sciences Center, Departments of Medicine and Biochemistry, Salt Lake City, Utah 84132

A mitochondrial matrix copper ligand (CuL) complex, conserved in mammalian cells, is the likely source of copper for assembly of cytochrome c oxidase (CcO) and superoxide dismutase 1 (Sod1) within the intermembrane space (IMS) in yeast. Targeting the copper-binding proteins human Sod1 and Crs5 to the mitochondrial matrix results in growth impairment on non-fermentable medium caused by decreased levels of CcO. This effect is reversed by copper supplementation. Matrix-targeted Crs5 diminished Sod1 protein within the IMS and impaired activity of an inner membrane tethered human Sod1. Copper binding by the matrix-targeted proteins attenuates levels of the CuL complex without affecting total mitochondrial copper. These data suggest that attenuation of the matrix CuL complex via heterologous competitors limits available copper for metallation of CcO and Sod1 within the IMS. The ligand also exists in the cytoplasm in an apparent metal-free state.

Received for publication, July 18, 2006 , and in revised form, September 27, 2006.

^* This work was supported by Grant ES03817 from the National Institutes of Health (to D. R. W.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: University of Utah Health Sciences Center, Salt Lake City, UT 84132. Tel.: 801-585-5103; Fax: 801-585-5469; E-mail: dennis.winge{at}hsc.utah.edu.

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