Catalysis in fumarate reductase

Graeme A Reid, Caroline S Miles, Ruth K Moysey, Katherine L Pankhurst, Stephen K Chapman

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    34 Citations (Scopus)

    Abstract

    In the absence of oxygen many bacteria are able to utilise fumarate as a terminal oxidant for respiration. In most known organisms the fumarate reductases are membrane-bound iron-sulfur flavoproteins but Shewanella species produce a soluble, periplasmic flavocytochrome c(3) that catalyses this reaction. The active sites of all fumarate reductases are clearly conserved at the structural level, indicating a common mechanism. The structures of fumarate reductases from two Shewanella species have been determined. Fumarate, succinate and a partially hydrated fumarate ligand are found in equivalent locations in different crystals, tightly bound in the active site and close to N5 of the FAD cofactor, allowing identification of amino acid residues that are involved in substrate binding and catalysis. Conversion of fumarate to succinate requires hydride transfer from FAD and protonation by an active site acid. The identity of the proton donor has been open to question but we have used structural considerations to suggest that this function is provided by an arginine side chain. We have confirmed this experimentally by analysing the effects of site-directed mutations on enzyme activity. Substitutions of Arg402 lead to a dramatic loss of activity whereas neither of the two active site histidine residues is required for catalysis. (C) 2000 Elsevier Science B.V. All rights reserved.

    Original languageEnglish
    Pages (from-to)310-315
    Number of pages6
    JournalBiochimica et Biophysica Acta - Bioenergetics
    Volume1459
    Issue number2-3
    DOIs
    Publication statusPublished - 15 Aug 2000
    Event11th European Bioenergetics Conference - BRIGHTON
    Duration: 9 Sep 200014 Sep 2000

    Keywords

    • C(3)
    • fumarate reductase
    • SEQUENCE
    • bacterial respiration
    • FRIGIDIMARINA NCIMB400
    • FLAVOCYTOCHROME-C
    • flavoprotein
    • ANAEROBIC RESPIRATION
    • MANGANESE
    • SHEWANELLA-PUTREFACIENS MR-1
    • Shewanella

    Cite this

    Reid, G. A., Miles, C. S., Moysey, R. K., Pankhurst, K. L., & Chapman, S. K. (2000). Catalysis in fumarate reductase. Biochimica et Biophysica Acta - Bioenergetics, 1459(2-3), 310-315. https://doi.org/10.1016/S0005-2728(00)00166-3