Reaction: an aldehyde + H2O + flavodoxin = a carboxylate + reduced flavodoxin
Other name(s): aldehyde oxidase; aldehyde oxidoreductase; Mop; AORDd
Systematic name: aldehyde:flavodoxin oxidoreductase (FAD-independent)
Comments: The enzyme, best characterized from the sulfate-reducing bacterium Megalodesulfovibrio gigas, belongs to the xanthine oxidase family of enzymes. However, it lacks the FAD-binding domain typically found in members of this family. Instead, it transfers electrons to flavodoxin, which fulfills the role of the missing domain. The enzyme contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) cofactor and two types of [2Fe-2S] clusters per monomer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:
References:
1. Romao, M.J., Barata, B.A., Archer, M., Lobeck, K., Moura, I., Carrondo, M.A., LeGall, J., Lottspeich, F., Huber, R. and Moura, J.J. Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers. Eur. J. Biochem. 215 (1993) 729-732. [PMID: 8354279]
2. Barata, B.A., LeGall, J. and Moura, J.J. Aldehyde oxidoreductase activity in Desulfovibrio gigas: in vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen. Biochemistry 32 (1993) 11559-11568. [PMID: 8218223]
3. Romao, M.J., Archer, M., Moura, I., Moura, J.J., LeGall, J., Engh, R., Schneider, M., Hof, P. and Huber, R. Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas. Science 270 (1995) 1170-1176. [PMID: 7502041]
4. Duarte, R.O., Archer, M., Dias, J.M., Bursakov, S., Huber, R., Moura, I., Romao, M.J. and Moura, J.J. Biochemical/spectroscopic characterization and preliminary X-ray analysis of a new aldehyde oxidoreductase isolated from Desulfovibrio desulfuricans ATCC 27774. Biochem. Biophys. Res. Commun. 268 (2000) 745-749. [PMID: 10679276]
5. Andrade, S.L., Brondino, C.D., Feio, M.J., Moura, I. and Moura, J.J. Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491. EPR assignment of the proximal [2Fe-2S] cluster to the Mo site. Eur. J. Biochem. 267 (2000) 2054-2061. [PMID: 10727945]
6. Rebelo, J.M., Dias, J.M., Huber, R., Moura, J.J. and Romao, M.J. Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å. J. Biol. Inorg. Chem. 6 (2001) 791-800. [PMID: 11713686]
7. Uchida, H., Kondo, D., Yamashita, A., Nagaosa, Y., Sakurai, T., Fujii, Y., Fujishiro, K., Aisaka, K. and Uwajima, T. Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690. FEMS Microbiol. Lett. 229 (2003) 31-36. [PMID: 14659539]
8. Krippahl, L., Palma, P.N., Moura, I. and Moura, J.JG. Modelling the electron-transfer complex between aldehyde oxidoreductase and flavodoxin. Eur J. Inorg. Chem. 2006 (2006) 3835-3840.