Startseite Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster
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Heterodisulfide reductase from methanogenic archaea: a new catalytic role for an iron-sulfur cluster

  • Reiner Hedderich , Nils Hamann und Marina Bennati
Veröffentlicht/Copyright: 12. Oktober 2005
Biological Chemistry
Aus der Zeitschrift Band 386 Heft 10

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.

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Published Online: 2005-10-12
Published in Print: 2005-10-01

©2005 by Walter de Gruyter Berlin New York

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