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Volume 271, Number 13, Issue of March 29, 1996 pp. 7719-7724
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
The Effect of Amino Acid Substitutions in the Conserved Aromatic Region of Subunit II of Cytochrome c Oxidase in Saccharomyces cerevisiae

(Received for publication, November 16, 1995; and in revised form, January 16, 1996)

Michael H. Overholtzer,  Peter S. Yakowec,  Vicki Cameron

Mitochondrial encoded subunit II of cytochrome c oxidase carries the metal center, which acts as the initial acceptor of electrons from cytochrome c. Among the conserved features of this protein is a region in which five aromatic and three non-aromatic amino acids are conserved in a wide variety of organisms. This aromatic region has been postulated to be involved in transfer of electrons from the copper center in subunit II to the remaining metal centers of cytochrome oxidase in subunit I. To test the functional importance of two conserved, aromatic tryptophan residues and one conserved, non-aromatic glycine residue, yeast strains with alterations at these positions were characterized. The strains with altered codons were tested for their ability to carry out cellular respiration, for their growth rates on non-fermentable carbon sources, and for their cytochrome c oxidase activity. The results demonstrate that the aromatic character of the tryptophan residues appears necessary for subunit II function, while the conserved glycine can be replaced with other, small, uncharged residues.



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This article has been cited by other articles:


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A.-X. Song, L.-Z. Li, T. Yu, S.-M. Chen, and Z.-X. Huang
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Tryptophan 121 of Subunit II Is the Electron Entry Site to Cytochrome-c Oxidase in Paracoccus denitrificans. INVOLVEMENT OF A HYDROPHOBIC PATCH IN THE DOCKING REACTION
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[Abstract] [Full Text] [PDF]


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Copyright © 1996 by the American Society for Biochemistry and Molecular Biology.