Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c
Related Experiment Video
Updated: Jul 30, 2026

A New Approach for the Comparative Analysis of Multiprotein Complexes Based on 15N Metabolic Labeling and Quantitative Mass Spectrometry
Published on: March 13, 2014
N Liang1, A G Mauk, G J Pielak
1Department of Chemistry, Northwestern University, Evanston, IL 60208.
Abstract:
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.
Related Concept Videos
Electron Transport Chains
The ETC is comprised of...
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
The Electron Transport Chain
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...
Electron Transport Chain: Complex III and IV
Electron Transport Chain Components

