Fumarate reductase

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Fumarate reductase respiratory complex
PDB 2bs3 EBI.jpg
Structure of Quinol-Fumarate Reductase Flavoprotein Subunit A.[1]
Identifiers
Symbol Fum_red_TM
Pfam PF01127
Pfam clan CL0335
InterPro IPR004224
SCOP 1qla
SUPERFAMILY 1qla
OPM superfamily 3
OPM protein 2bs3
CDD cd03494
Fumarate reductase subunit C
PDB 1l0v EBI.jpg
quinol-fumarate reductase with menaquinol molecules
Identifiers
Symbol Fumarate_red_C
Pfam PF02300
Pfam clan CL0335
InterPro IPR003510
SCOP 1fum
SUPERFAMILY 1fum
CDD cd00546
Fumarate reductase subunit D
PDB 1kfy EBI.jpg
quinol-fumarate reductase with quinol inhibitor 2-[1-(4-chloro-phenyl)-ethyl]-4,6-dinitro-phenol
Identifiers
Symbol Fumarate_red_D
Pfam PF02313
Pfam clan CL0335
InterPro IPR003418
SCOP 1fum
SUPERFAMILY 1fum
CDD cd00547

Fumarate reductase is the enzyme that converts fumarate to succinate, and is important in microbial metabolism as a part of anaerobic respiration.[2]

Succinate + 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).[3]

Fumarate reductase complex includes four subunits.[4] 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.[3] The D subunit may be required to anchor the catalytic components of the fumarate reductase complex to the cytoplasmic membrane.

See also[edit]

References[edit]

  1. ^ Lancaster CR, Sauer US, Gross R, et al. (December 2005). "Experimental support for the "E pathway hypothesis" of coupled transmembrane e- and H+ transfer in dihemic quinol:fumarate reductase". Proc. Natl. Acad. Sci. U.S.A. 102 (52): 18860–5. doi:10.1073/pnas.0509711102. PMC 1323215Freely accessible. PMID 16380425. 
  2. ^ Iverson TM, Luna-Chavez C, Cecchini G, Rees DC (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex". Science. 284 (5422): 1961–6. doi:10.1126/science.284.5422.1961. PMID 10373108. 
  3. ^ a b Michel H, Lancaster CR, Kroger A, Auer M (1999). "Structure of fumarate reductase from Wolinella succinogenes at 2.2 A resolution". Nature. 402 (6760): 377–385. doi:10.1038/46483. PMID 10586875. 
  4. ^ Iverson, T. M.; Luna-Chavez, C; Cecchini, G; Rees, D. C. (1999). "Structure of the Escherichia coli fumarate reductase respiratory complex". Science. 284 (5422): 1961–6. doi:10.1126/science.284.5422.1961. PMID 10373108. 

External links[edit]

This article incorporates text from the public domain Pfam and InterPro IPR004224

This article incorporates text from the public domain Pfam and InterPro IPR003510

This article incorporates text from the public domain Pfam and InterPro IPR003418