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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1974 Jun;71(6):2539–2543. doi: 10.1073/pnas.71.6.2539

Homology Between Bakers' Yeast Cytochrome b2 and Liver Microsomal Cytochrome b5*

B Guiard 1, O Groudinsky 1, F Lederer 1,†
PMCID: PMC388495  PMID: 4210211

Abstract

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.

Keywords: amino-acid sequence, protein structure, electron transfer, evolution

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Selected References

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