Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c

Nong Liang*, A. Grant Mauk, Gary J. Pielak, Jeanette A. Johnson, Michael Smith, Brian M. Hoffman

*Corresponding author for this work

Research output: Contribution to journalArticle

108 Scopus citations

Abstract

Yeast iso-l-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 ∼104 slower at ∼0°C than for the two variants with aromatic residues.

Original languageEnglish (US)
Pages (from-to)311-313
Number of pages3
JournalScience
Volume240
Issue number4850
DOIs
StatePublished - 1988

ASJC Scopus subject areas

  • General

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