期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1974
卷号：71
期号：6
页码：2539-2543
DOI：10.1073/pnas.71.6.2539
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The amino-acid sequence of the hemebinding region of bakers' yeast cytochrome b2 [L-(+)-lactate dehydrogenase, EC 1.1.2.3 ] has been determined. It shows a strong similarity with the sequence of microsomal cytochrome b5, and appears to be compatible with the same kind of peptide-chain folding, in agreement with data obtained previously by various physiochemical methods. The comparison shows that the fifth and sixth heme ligands must be histidine residues, thus substantiating previous conclusions drawn in particular from photooxidation experiments and nuclear magnetic resonance studies. The data reported in this paper suggest a common origin for the two proteins. Implications for their biochemical evolution are presented.
关键词：amino-acid sequence ; protein structure ; electron transfer ; evolution
