The amino acid sequence of cytochrome c of Neurospora crassa.
- 1 December 1965
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 54 (6) , 1621-1625
- https://doi.org/10.1073/pnas.54.6.1621
Abstract
The complete amino acid sequence of N. crassa cytochrome c is reported. The cytochromes c from "wild type" and a maternally inherited mutant mi-1 ("poky") are identical. The protein consists of a single polypeptide chain containing 107 residues. The molecule contains 2 histidine residues in positions 18 and 33 and lacks the histidine residue usually found at position 26. It is suggested that the 6th ligand of the heme Fe in cytochrome c may be either an oxygen (glutamyl or tyrosyl) or the indole of tryptophan.This publication has 10 references indexed in Scilit:
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