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

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

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

M Nakai,H Ishiwatari,A Asada,M Bogaki,K Kawai,Y Tanaka,H Matsubara,

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 encoding the Phe-44, Tyr-44, Leu-164, or Lys-164 protein, none of these transformants could grow on the non-fermentable carbon source. These results suggest that the His-44 and Met-164 residues have a critical role in the function of cytochrome c1 in vivo, most probably as axial ligands of the heme iron. Further analysis revealed that the mutant yeast cells with the Phe-44, Tyr-44, or Leu-164 protein lacked the characteristic difference spectroscopic signal of cytochrome c1. However, in the Lys-164 mutant cells, partial recovery of the cytochrome c1 signal was observed. Moreover, the Lys-164 protein retained a low but significant level of succinate-cytochrome c reductase activity in vitro. The possibility that the nitrogen of Lys-164 served as the sixth heme ligand is discussed in comparison with cytochrome f of a photosynthetic electron-transfer complex, in which lysine has been proposed to be the sixth ligand.

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

M Nakai,H Ishiwatari,A Asada,M Bogaki,K Kawai,Y Tanaka,H Matsubara,

For similar investigative techniques: chemistry, analytical: crystallography: x-ray diffraction research abstracts see: investigative techniques: chemistry, analytical: crystallography: x-ray diffraction research

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

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 108

Page Numbers: 798-803

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Nov

YEAR: 1990

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

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LANGUAGE: eng

NlmUniqueID: 376600

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

KEYWORDS: X-Ray Diffraction

MESH TERMS: genetics

Chemical & Substance for Abstract: Replacement of putative axial ligands of heme iron in yeast cytochrome c1 by site-directed mutagenesis. Information

Substance Name: Cytochromes c1

Registry Number: 9035-42-1

Grant and Affiliation Information for Replacement of putative axial ligands of heme iron in yeast cytochrome c1 by site-directed mutagenesis.

AFFILIATION: Department of Biology, Faculty of Science, Osaka University.

Country: JAPAN

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MEDLINETA: J Biochem

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