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Fumarate reductase
Fumarate reductase is the enzyme that converts fumarate to succinate, it is important in microbial metabolism as a means for anaerobic respiration.[1] Additional recommended knowledgeSuccinate + acceptor <=> fumarate + reduced acceptor In other words, fumarate reductase couples the reduction of fumarate to succinate to the oxidation of quinol to quinone, in a reaction opposite to that catalysed by the related complex II of the respiratory chain (succinate dehydrogenase)[2]. Fumarate reductase complex includes three subunits. Subunit A contains the site of fumarate reduction and a covalently bound flavin adenine dinucleotide prosthetic group. Subunit B contains three iron-sulphur centres. The menaquinol-oxidizing subunit C consists of five membrane-spanning, primarily helical segments and binds two haem b molecules[2]. See alsoReferences
This article includes text from the public domain Pfam and InterPro IPR004224 Categories: Enzymes | Protein domains | Transmembrane proteins |
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This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Fumarate_reductase". A list of authors is available in Wikipedia. |