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Alternative oxidase information


The alternative oxidase shown as part of the complete electron transport chain. UQ is ubiquinol/ubiquinone, C is cytochrome c and AOX is the alternative oxidase.
Alternative oxidase
Identifiers
SymbolAOX
PfamPF01786
InterProIPR002680
OPM superfamily357
OPM protein3w54
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Also matches plastid terminal oxidase and bacterial AOX.

The alternative oxidase (AOX) is an enzyme that forms part of the electron transport chain in mitochondria of different organisms.[1][2] Proteins homologous to the mitochondrial oxidase and the related plastid terminal oxidase have also been identified in bacterial genomes.[3][4]

The oxidase provides an alternative route for electrons passing through the electron transport chain to reduce oxygen. However, as several proton-pumping steps are bypassed in this alternative pathway, activation of the oxidase reduces ATP generation. This enzyme was first identified as a distinct oxidase pathway from cytochrome c oxidase as the alternative oxidase is resistant to inhibition by the poison cyanide.[5]

  1. ^ McDonald A, Vanlerberghe G (2004). "Branched mitochondrial electron transport in the Animalia: presence of alternative oxidase in several animal phyla". IUBMB Life. 56 (6): 333–41. doi:10.1080/1521-6540400000876. PMID 15370881.
  2. ^ Sluse FE, Jarmuszkiewicz W (1998). "Alternative oxidase in the branched mitochondrial respiratory network: an overview on structure, function, regulation, and role". Braz. J. Med. Biol. Res. 31 (6): 733–47. doi:10.1590/S0100-879X1998000600003. PMID 9698817.
  3. ^ McDonald AE, Amirsadeghi S, Vanlerberghe GC (2003). "Prokaryotic orthologues of mitochondrial alternative oxidase and plastid terminal oxidase". Plant Mol. Biol. 53 (6): 865–76. doi:10.1023/B:PLAN.0000023669.79465.d2. PMID 15082931. S2CID 41525108.
  4. ^ Atteia A, van Lis R, van Hellemond JJ, Tielens AG, Martin W, Henze K (2004). "Identification of prokaryotic homologues indicates an endosymbiotic origin for the alternative oxidases of mitochondria (AOX) and chloroplasts (PTOX)". Gene. 330: 143–8. doi:10.1016/j.gene.2004.01.015. PMID 15087133.
  5. ^ Moore AL, Siedow JN (1991). "The regulation and nature of the cyanide-resistant alternative oxidase of plant mitochondria". Biochim. Biophys. Acta. 1059 (2): 121–40. doi:10.1016/S0005-2728(05)80197-5. PMID 1883834.

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