Replacement of putative axial ligands of heme iron in yeast cytochrome c1 by site-directed mutagenesis.

@article{Nakai1990ReplacementOP,
  title={Replacement of putative axial ligands of heme iron in yeast cytochrome c1 by site-directed mutagenesis.},
  author={Masato Nakai and Haruko Ishiwatari and Akikazu Asada and M Bogaki and Kiyoshi Kawai and Yoko Tanaka and Hiroshi Matsubara},
  journal={Journal of biochemistry},
  year={1990},
  volume={108 5},
  pages={798-803}
}
The His-44 and Met-164 residues of yeast cytochrome c1 are evolutionally conserved and regarded as heme axial ligands bonding to the fifth and sixth coordination sites of the heme iron, which is directly involved in the electron transfer mechanism. Oligonucleotide-directed mutagenesis was used to generate mutant forms of cytochrome c1 of yeast having amino acid replacements of the putative axial ligands of the heme iron. When a cytochrome c1-deficiency yeast strain was transformed with a gene… CONTINUE READING