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multicopper oxidase domain-containing protein
This entry contains many divergent copper oxidase-like domains that are not recognised by the Pfam:PF00394 model. [1]. 2404764. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Messerschmidt A, Huber R;. Eur J Biochem 1990;187:341-352. [2]. 1548698. Refined crystal structure of ascorbate oxidase at 1.9 A resolution. Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agro A;. J Mol Biol 1992;224:179-205. [3]. 10573417. Natural engineering principles of electron tunnelling in biological oxidation-reduction. Page CC, Moser CC, Chen X, Dutton PL;. Nature 1999;402:47-52. [4]. 7599131. X-ray absorption studies and homology modeling define the structural features that specify the nature of the copper site in rusticyanin. Grossmann JG, Ingledew WJ, Harvey I, Strange RW, Hasnain SS;. Biochemistry 1995;34:8406-8414. (from Pfam)
Multicopper oxidase
Many of the proteins in this family contain multiple similar copies of this plastocyanin-like domain. [1]. 2404764. The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. Messerschmidt A, Huber R;. Eur J Biochem 1990;187:341-352. [2]. 1548698. Refined crystal structure of ascorbate oxidase at 1.9 A resolution. Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agro A;. J Mol Biol 1992;224:179-205. (from Pfam)
multicopper oxidase family protein
multicopper oxidase family protein couples the one-electron oxidation of four substrate molecules to the four electron reductive cleavage of the O-O bond of dioxygen
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