Journal
BIOLOGICAL CHEMISTRY
Volume 386, Issue 10, Pages 961-970Publisher
WALTER DE GRUYTER & CO
DOI: 10.1515/BC.2005.112
Keywords
disulfide reductase; ferredoxin : thioredoxin reductase; heterodisulfide reductase; iron-sulfur proteins; methanogenic archaea
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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.
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