3vr8
From Proteopedia
Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum
Structural highlights
FunctionSDHA1_ASCSU Flavoprotein (Fp) subunit of the mitochondrial electron transport chain complex II which, together with the iron-sulfur protein (Ip) subunit forms the catalytic core of the complex (PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7739664, PubMed:7822332, PubMed:8435436). During the parasitic larvae and adult stages, which occur in an anaerobic environment, acts as a fumarate reductase by transferring electrons from rhodoquinol to fumarate (PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7739664, PubMed:7822332, PubMed:8435436).[1] [2] [3] [4] [5] [6] Publication Abstract from PubMedIn the anaerobic respiratory chain of the parasitic nematode Ascaris suum, complex II couples the reduction of fumarate to the oxidation of rhodoquinol, a reverse reaction catalyzed by mammalian complex II. In this study, the first structure of anaerobic complex II of mitochondria was determined. The structure, composed of four subunits and five co-factors, is similar to that of aerobic complex II, except for an extra peptide found in the smallest anchor subunit of the A. suum enzyme. We discuss herein the structure-function relationship of the enzyme and the critical role of the low redox potential of rhodoquinol in the fumarate reduction of A. suum complex II. Crystal structure of mitochondrial quinol-fumarate reductase from the parasitic nematode Ascaris suum.,Shimizu H, Osanai A, Sakamoto K, Inaoka DK, Shiba T, Harada S, Kita K J Biochem. 2012 Jun;151(6):589-92. Epub 2012 May 9. PMID:22577165[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations 8 reviews cite this structure No citations found See AlsoReferences
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Categories: Ascaris suum | Large Structures | Harada S | Inaoka DK | Kita K | Osanai A | Sakamoto K | Shiba T | Shimizu H