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. 1983 Sep 1;213(3):687–700. doi: 10.1042/bj2130687

The conformation of eukaryotic cytochrome c around residues 39, 57, 59 and 74.

M N Robinson, A P Boswell, Z X Huang, C G Eley, G R Moore
PMCID: PMC1152184  PMID: 6311172

Abstract

1H-n.m.r. studies of horse, tuna, Candida krusei and Saccharomyces cerevisiae cytochromes c showed that each of the proteins contains a similar cluster of residues at the bottom of the protein that assists in shielding the haem from the solvent. The relative positions of the residues forming these clusters vary continuously with temperature, and they change with the change in protein redox state. This conformational heterogeneity is discussed with reference to the conformational flexibility of cytochrome c around residues 57, 59 and 74. Spectroscopic measurements of pKa values for Lys-55 (horse and tuna cytochromes c) and His-33 and His-39 (C. krusei and S. cerevisiae cytochromes c) are in excellent agreement with expectations based on chemical-modification studies of horse cytochrome c. [Bosshard & Zürrer (1980) J. Biol. Chem. 255, 6694-6699] and on the X-ray-crystallographic structure of tuna cytochrome c [Takano & Dickerson (1981) J. Mol. Biol. 153, 79-94, 95-115].

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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