Anaerobic respiration with elemental sulfur and with disulfides

Authors

  • Reiner Hedderich,

    Corresponding author
    1. Max-Planck-Institut für terrestrische Mikrobiologie and Laboratorium für Mikrobiologie des Fachbereichs Biologie der Philipps-Universität, Karl-von-Frisch-Straße, D-35043 Marburg, Germany
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  • Oliver Klimmek,

    1. Institut für Mikrobiologie der Johann-Wolfgang-Goethe-Universität Frankfurt am Main, Marie-Curie-Straße 9, D-60439 Frankfurt am Main, Germany
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  • Achim Kröger,

    1. Institut für Mikrobiologie der Johann-Wolfgang-Goethe-Universität Frankfurt am Main, Marie-Curie-Straße 9, D-60439 Frankfurt am Main, Germany
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  • Reinhard Dirmeier,

    1. Lehrstuhl für Mikrobiologie, Universität Regensburg, Universitätsstraße 31, D-93053 Regensburg, Germany
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  • Martin Keller,

    1. Lehrstuhl für Mikrobiologie, Universität Regensburg, Universitätsstraße 31, D-93053 Regensburg, Germany
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  • Karl O. Stetter

    1. Lehrstuhl für Mikrobiologie, Universität Regensburg, Universitätsstraße 31, D-93053 Regensburg, Germany
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*Corresponding author. Tel.: +49 (6421) 178230; Fax: +49 (6421) 178299; E-mail: hedderic@mailer.uni-marburg.de

Abstract

Anaerobic respiration with elemental sulfur/polysulfide or organic disulfides is performed by several bacteria and archaea, but has only been investigated in a few organisms in detail. The electron transport chain that catalyzes polysulfide reduction in the Gram-negative bacterium Wolinella succinogenes consists of a dehydrogenase (formate dehydrogenase or hydrogenase) and polysulfide reductase. The enzymes are integrated in the cytoplasmic membrane with the catalytic subunits exposed to the periplasm. The mechanism of electron transfer from formate dehydrogenase or hydrogenase to polysulfide reductase is discussed. The catalytic subunit of polysulfide reductase belongs to the family of molybdopterin-dinucleotide-containing oxidoreductases. From the hyperthermophilic archaeon Pyrodictium abyssi isolate TAG11 an integral membrane complex has been isolated which catalyzes the reduction of sulfur with H2 as electron donor. This enzyme complex, which is composed of a hydrogenase and a sulfur reductase, contains heme groups and several iron-sulfur clusters, but does not contain molybdenum or tungsten. In methanogenic archaea, the heterodisulfide of coenzyme M and coenzyme B is the terminal electron acceptor of the respiratory chain. In methanogens belonging to the order Methanosarcinales, this respiratory chain is composed of a dehydrogenase, the membrane-soluble electron carrier methanophenazine, and heterodisulfide reductase. The catalytic subunit of heterodisulfide reductase contains only iron-sulfur clusters. An iron-sulfur cluster may directly be involved in the reduction of the disulfide substrate.

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