
Amino acid sequences of bacterial cytochromes c' and c-556.
Author(s) -
R. P. Ambler,
Robert G. Bartsch,
M Daniel,
Martin D. Kamen,
Lesley I. McLellan,
T.E. Meyer,
Jozef Van Beeumen
Publication year - 1981
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.78.11.6854
Subject(s) - heme , cytochrome , biochemistry , hemeprotein , cytochrome c , amino acid , electron transport chain , bacteria , chemistry , methionine , biology , stereochemistry , mitochondrion , enzyme , genetics
The cytochrome c' are electron transport proteins widely distributed in photosynthetic and aerobic bacteria. We report the amino acid sequences of the proteins from 12 different bacterial species, and we show by sequences that the cytochromes c-556 from 2 different bacteria are structurally related to the cytochromes c'. Unlike the mitochondrial cytochromes c, the heme binding site in the cytochromes c' and c-556 is near the COOH terminus. The cytochromes c-556 probably have a methionine sixth heme ligand located near the NH2 terminus, whereas the cytochromes c' may be pentacoordinate. Quantitative comparison of cytochrome c' and c-556 sequences indicates a relatively low 28% average identity.