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Reiner Hedderich, Nils Hamann, Marina Bennati
Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
Keywords: disulfide reductase, ferredoxin:thioredoxin reductase, heterodisulfide reductase, iron-sulfur proteins, methanogenic archaea
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.
Biological Chemistry, Walter de Gruyter
Print ISSN: 1431-6730
Volume: 386, 10/2005
Pages: 961 - 970