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J. Biol. Chem., Vol. 280, Issue 18, 17652-17656, May 6, 2005

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Assembly of Cytochrome-c Oxidase in the Absence of Assembly Protein Surf1p Leads to Loss of the Active Site Heme^*

Daniel Smith, Jimmy Gray, Larkin Mitchell, William E. Antholine, and Jonathan P. Hosler¶

From the Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216-4505 and the National Biomedical ESR Center, Department of Biophysics, Medical College of Wisconsin, Milwaukee, Wisconsin 53226-3548

Surf1p is a protein of the inner membrane of mitochondria that functions in the assembly of cytochrome-c oxidase. The specifics of the role of Surf1p have remained unresolved. Numerous mutations in human Surf1p lead to severe mitochondrial disease. A homolog of human Surf1p is encoded by the genome of the -proteobacterium Rhodobacter sphaeroides, which synthesizes a mitochondrial-like aa₃-type cytochrome-c oxidase. The gene for Surf1p was deleted from the genome of R. sphaeroides. The resulting aa₃-type oxidase was purified and analyzed by biochemical methods plus optical and EPR spectroscopy. The oxidase that assembled in the absence of Surf1p was composed of three subpopulations with structurally distinct heme a₃-Cu active sites. 50% of the oxidase lacked heme a₃, 10–15% contained heme a₃ but lacked Cu_BB, and 35–40% had a normal heme a₃ -Cu_B active site with normal activity. Cu_A assembly was unaffected. All of the oxidase contained low-spin heme a, but the environment of the heme a center was slightly altered in the 50% of the enzyme that lacked heme a₃. Introduction of a normal copy of the gene for Surf1p on an exogenous plasmid resulted in a single population of normally assembled, highly active enzyme. The data indicate that Surf1p plays a role in facilitating the insertion of heme a₃ into the active site of cytochrome-c oxidase. The results suggest that maturation of the heme a₃-Cu_B center is a step that limits the association of subunits I and II in the assembly of mitochondrial cytochrome oxidase.

Received for publication, February 14, 2005 , and in revised form, March 8, 2005.

^* This work was supported by National Institutes of Health Grants GM56824 (to J. P. H.) and EB001980 (to W. E. A.) and by Grant DE-FG02-01ER63232 from the U. S. Department of Energy (to J. P. H.). 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.

The nucleotide sequence(s) reported in this paper has been submitted to GenBank^TM/EBI Data Bank with the accession number(s) AY918925.

^¶ To whom correspondence should be addressed: Dept. of Biochemistry, University of Mississippi Medical Center, 2500 N. State St., Jackson, MS 39216-4505. Tel.: 601-984-1861; Fax: 601-984-1501; E-mail: jhosler{at}biochem.umsmed.edu.

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