Related Experiment Video
Updated: Aug 15, 2026

EPR Monitored Redox Titration of the Cofactors of Saccharomyces cerevisiae Nar1
Published on: November 26, 2014
Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
Reiner Hedderich1, Nils Hamann, Marina Bennati
1Max-Planck-Institute for Terrestrial Microbiology, Karl-von-Frisch Strasse, D-35043 Marburg, Germany. hedderic@staff.uni-marburg.de
Abstract:
Heterodisulfide reductase (HDR) from methanogenic archaea is an iron-sulfur protein that catalyzes reversible reduction of the heterodisulfide (CoM-S-S-CoB) of the methanogenic thiol-coenzymes, coenzyme M (CoM-SH) and coenzyme B (CoB-SH). Via the characterization of a paramagnetic reaction intermediate generated upon oxidation of the enzyme in the presence of coenzyme M, the enzyme was shown to contain a [4Fe-4S] cluster in its active site that catalyzes reduction of the disulfide substrate in two one-electron reduction steps. The formal thiyl radical generated by the initial one-electron reduction of the disulfide is stabilized via reduction and coordination of the resultant thiol to the [4Fe-4S] cluster.
More Related Videos
06:52Experimental Column Setup for Studying Anaerobic Biogeochemical Interactions Between Iron (Oxy)Hydroxides, Trace Elements, and Bacteria
Published on: December 19, 2017
10:01Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
Related Concept Videos
Sulfur Assimilation
Microbes and Other Elemental Cycles
Diversity of Archaea III
Microbes and the Sulfur Cycle
Anoxygenic Photosynthesis
Microbial Nutrition