Related Experiment Video
Updated: Jul 4, 2026

Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
Published on: March 18, 2012
Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase
M H Charon1, A Volbeda, E Chabriere
1Laboratoire de Cristallographie et de Cristallogenèse des Protéines, Institut de Biologie Structurale J-P Ebel (CEA, CNRS), Grenoble, 38027, France. charon@ibs.fr
Abstract:
The first crystal structure of pyruvate:ferredoxin oxidoreductase to be determined has provided significant new information on its structural organization and redox chemistry. Spectroscopic analyses of a radical reaction intermediate have shed more light on its thiamin-based mechanism of catalysis. Different approaches have been used to study the interaction between the enzyme and ferredoxin, its redox partner.
More Related Videos
08:57Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
10:21Expression, Purification, Crystallization, and Enzyme Assays of Fumarylacetoacetate Hydrolase Domain-Containing Proteins
Published on: June 20, 2019
Related Concept Videos
Redox Reactions
Pyruvate Oxidation
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
Electron Transport Chains
The ETC is comprised of...
Electron Transport Chain: Complex I and II
ROS generation is regulated and maintained at moderate levels necessary...
Role of Reduced Coenzymes NADH and FADH₂
Redox Reactions