Publication Date:
1988-04-15
Description:
Yeast iso-1-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)+,FeIICc] converts to [ZnCcP,FeIIICc] by a single, intracomplex electron transfer step that is not governed by "gating" through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by FeIICc subsequent to its formation from FeIIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is approximately 10(4) slower at approximately 0 degrees C than for the two variants with aromatic residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liang, N -- Mauk, A G -- Pielak, G J -- Johnson, J A -- Smith, M -- Hoffman, B M -- GM-33804/GM/NIGMS NIH HHS/ -- HL-13531/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):311-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832950" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acids
;
Cytochrome c Group/*metabolism
;
Cytochrome-c Peroxidase/*metabolism
;
*Cytochromes c
;
Electron Transport
;
Genetic Variation
;
Kinetics
;
Peroxidases/*metabolism
;
Photolysis
;
Saccharomyces cerevisiae/metabolism
;
*Saccharomyces cerevisiae Proteins
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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