Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein |
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| Authors: | Cutler, R.L. Pielak, G.J. Mauk, A. G. Smith, M. |
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| Affiliation: | Department of Biochemistry, University of British Columbia 2146 Health Sciences Mall, Vancouver, British Columbia V6T 1W5, Canada 1Inorganic Chemistry Laboratory, University of Oxford South Parks Road, Oxford OX1 3QR, UK |
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| Abstract: | Site-directed mutagenesis has been used to change the codonfor cysteine-107 of Saccharomyces cerevisiae iso-1-cytochromec to a threonine codon. The resulting protein is active in vivo,is methylated as in the wild-type protein and has optical propertiesindistinguishable from those of the wild-type protein. The threonine-107iso-1-cytochrome c demonstrated fully reversible electrochemicalbehaviour and a mid-point reduction potential of 272 mV versusNHE. In addition, this mutant does not demonstrate a tendencyto autoreduce or to dimerize as does the wild-type protein.These properties of the threonine-107 mutant establish thatit will provide a useful background in which to make subsequentmutations for mechanistic and physical studies of yeast iso-1-cytochromec. |
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| Keywords: | iso-1-cytochrome c/ reduction potential/ site-directed mutagenesis |
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