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Biochimie. 1994;76(7):622-30.

Strategies for the study of cytochrome c structure and function by site-directed mutagenesis.

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Institut de Biologie Structurale, Grenoble, France.


The class I cytochromes c have been extensively studied by biochemical and biophysical methods; however, many questions remain concerning the roles of specific amino acids in electron transfer and stability properties. The method of site-directed mutagenesis, which substitutes specific amino acid residues by genetic methods, is ideal for addressing these questions of cytochrome c structure and function. Practical considerations of mutational effects on protein processing and stability will be addressed. The criteria for the selection of mutation sites will be discussed. Examples of site-directed mutagenesis studies, which were designed to elucidate the factors controlling biological electron transfer, protein processing, and protein stability, are given.

[Indexed for MEDLINE]

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