User:Estelle Blochouse/ Sandbox 1497

Multicopper oxidases are enzymes involved in copper homeostasis. Copper as many metal ions is used in multiple biological processes such as detoxification of oxygen free radicals and pigmentation. However copper present in a cell bot bounded to a protein if harmfull and can cause cellular damage. It need to be regulated.

Multicopper oxidases are abble to oxiise their substrate. They accept an electron in the <scene name='pdbligand=CU:COPPER+(II)+ION'>mononoclear copper center</scene> and transfer it to the trinuclear copper centre. The dioxygen bind to the trinuclear center and recieve four electron. It is transformed into two molecules of water.<ref name="pmid16234932">{{cite journal | vauthors = Bento I, Martins LO, Gato Lopes G, Arménia Carrondo M, Lindley PF | title = Dioxygen reduction by multi-copper oxidases; a structural perspective | journal = [[Dalton Transactions]] | volume = | issue = 21 | pages = 3507–13 |date=November 2005 | pmid = 16234932 | doi = 10.1039/b504806k | url = }}</ref> Three copper centres exist that can be differentiate spectroscopically: Type 1 or blue (<scene name='pdbligand=CU:COPPER+(II)+ION'>mononoclear copper center</scene>), type 2 or normal (Cu1004) and type 3 or coupled binuclear (1002 and 1003).<ref name="pmid2404764">{{cite journal | vauthors = Messerschmidt A, Huber R | title = The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships | journal = Eur. J. Biochem. | volume = 187 | issue = 2 | pages = 341–52 |date=January 1990 | pmid = 2404764 | doi = 10.1111/j.1432-1033.1990.tb15311.x | url = }}</ref><ref name="pmid1995346">{{cite journal | vauthors = Ouzounis C, Sander C | title = A structure-derived sequence pattern for the detection of type I copper binding domains in distantly related proteins | journal = FEBS Lett. | volume = 279 | issue = 1 | pages = 73–8 |date=February 1991 | pmid = 1995346 | doi = 10.1016/0014-5793(91)80254-Z| url = }}</ref>