J. Biochem, 1990, Vol. 108, No. 1 7-8
© 1990 Japanese Biochemical Society
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Site-Directedly Mutated Human Cytochrome c Which Retains Heme c via Only One Thioether Bond
*Institute for Fundamental Research, Research Center, Suntory Ltd. Shimamoto-cho, Mishima-gun, Osaka 618
**Bio-Pharma Tech. Center, Suntory Ltd. Chiyoda-cho, Oura-gun, Gunma 370-05
***Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka 560
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) Biochenm. J. 147, 291–302].
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