CMulti-copper polyphenol oxidoreductase laccase
crystal structure of protein cc_0490 from caulobacter crescentus, pfam duf152
In molecular biology,
multicopper oxidases are enzymes which oxidise their substrate by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear copper centre; dioxygen binds to the trinuclear centre and, following the transfer of four electrons, is reduced to two molecules of water. There are three  spectroscopically different copper centres found in multicopper oxidases: type 1 (or blue), type 2 (or normal) and type 3 (or coupled binuclear).  Multicopper oxidases consist of 2, 3 or 6 of these  homologous domains, which also share homology with the cupredoxins azurin and plastocyanin. Structurally, these domains consist of a cupredoxin-like fold, a beta-sandwich consisting of 7 strands in 2 beta-sheets, arranged in a Greek-key beta-barrel. Multicopper oxidases include: 
In addition to the above
enzymes there are a number of other proteins that are similar to the multi-copper oxidases in terms of structure and sequence, some of which have lost the ability to bind copper. These include: copper resistance protein A (copA) from a plasmid in ; domain A of (non-copper binding) Pseudomonas syringae blood coagulation factors V (Fa V) and VIII (Fa VIII);  yeast Fet3p (FET3) required for ferrous iron uptake;  yeast hypothetical protein YFL041w; and the fission yeast homologue SpAC1F7.08.
References [ edit ]
^ Bento I, Martins LO, Gato Lopes G, Arménia Carrondo M, Lindley PF (November 2005). "Dioxygen reduction by multi-copper oxidases; a structural perspective". (21): 3507–13. Dalton Transactions PMID 16234932. doi: 10.1039/b504806k.
^ Messerschmidt A, Huber R (January 1990). "The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships". Eur. J. Biochem. 187 (2): 341–52. PMID 2404764. doi: 10.1111/j.1432-1033.1990.tb15311.x.
^ Ouzounis C, Sander C (February 1991). "A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins". FEBS Lett. 279 (1): 73–8. PMID 1995346. doi: 10.1016/0014-5793(91)80254-Z.
^ a b Roberts SA, Weichsel A, Grass G, Thakali K, Hazzard JT, Tollin G, Rensing C, Montfort WR (March 2002). "Crystal structure and electron transfer kinetics of CueO, a multicopper oxidase required for copper homeostasis in Escherichia coli". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2766–71. PMC . 122422 PMID 11867755. doi: 10.1073/pnas.052710499.
^ Nakamura K, Kawabata T, Yura K, Go N (October 2003). "Novel types of two-domain multi-copper oxidases: possible missing links in the evolution". FEBS Lett. 553 (3): 239–44. PMID 14572631. doi: 10.1016/S0014-5793(03)01000-7.
^ Suzuki S, Kataoka K, Yamaguchi K (October 2000). "Metal coordination and mechanism of multicopper nitrite reductase". Acc. Chem. Res. 33 (10): 728–35. PMID 11041837. doi: 10.1021/ar9900257.
^ Mann KG, Jenny RJ, Krishnaswamy S (1988). "Cofactor proteins in the assembly and expression of blood clotting enzyme complexes". Annu. Rev. Biochem. 57: 915–56. PMID 3052293. doi: 10.1146/annurev.bi.57.070188.004411.
^ Askwith C, Eide D, Van Ho A, Bernard PS, Li L, Davis-Kaplan S, Sipe DM, Kaplan J (January 1994). "The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake". Cell. 76 (2): 403–10. PMID 8293473. doi: 10.1016/0092-8674(94)90346-8.
This article incorporates text from the public domain Pfam and InterPro IPR001117
This article incorporates text from the public domain Pfam and InterPro IPR011706
This article incorporates text from the public domain Pfam and InterPro IPR011707
This article incorporates text from the public domain Pfam and InterPro IPR003730