Site-directedly mutated human cytochrome c which retains heme c via only one thioether bond |
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Authors: | Y Tanaka I Kubota T Amachi H Yoshizumi H Matsubara |
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Institution: | Institute for Fundamental Research, Research Center, Suntory Ltd., Osaka. |
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Abstract: | Although Cys-14 (human numbering) of cytochrome c was conserved during its molecular evolution and it is supposed to be essential for most cytochromes c to retain heme c via two thioether bonds, a site-directedly mutated human cytochrome c which has an alanine residue at this position and only one thioether bond through Cys-17 turns out to be functional. This shows that Cys-14 is not essential. The absorption spectrum of the atypical cytochrome c is red shifted, and similar to those of Euglena and Crithidia cytochromes c, which also have only one thioether bond Pettigrew, G.W., Leaver, J.L., Meyer, T.E., & Ryle, A.P. (1975) Biochem. J. 147, 291-302]. |
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