Related Experiment Video
Updated: Jan 13, 2026

Inner Mitochondrial Membrane Sensitivity to Na+ Reveals Partially Segmented Functional CoQ Pools
Published on: July 20, 2022
Control of cytochrome c redox reactivity through off-pathway modifications in the protein hydrogen-bonding network
Jie Gu1, Soyeun Yang, Alexander J Rajic
1Department of Chemistry, Dartmouth College, Hanover, NH 03755, USA. ekaterina.pletneva@dartmouth.edu.
Abstract:
Measurements of photoinduced Fe(2+)-to-Ru(3+) electron transfer (ET), supported by theoretical analysis, demonstrate that mutations off the dominant ET pathways can strongly influence the redox reactivity of cytochrome c. The effects arise from the change in the protein dynamics mediated by the intraprotein hydrogen-bonding network.
More Related Videos
07:16Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Published on: June 21, 2021
10:24Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
Published on: June 7, 2018