Strategies for the study of cytochrome c structure and function by site-directed mutagenesis.
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.
Caffrey
M S
MS
Institut de Biologie Structurale, Grenoble, France.
D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000378:metabolism; D016384:Consensus Sequence; D003574:Cytochrome c Group / Q000737:chemistry* / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000378:metabolism; D008961:Models, Structural; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017433:Protein Structure, Secondary; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism
D003574:Cytochrome c Group; D011994:Recombinant Proteins