Blue Copper Oxidases A. Messerschmidt

Messerschmidt A (1988) Metal Sites in Small Blue Copper Proteins, Blue Copper Oxidases and Vanadium-Containing Enzymes. 90 37-68 Michel H, see Hemmerich P (1982) 48 93-124... 

Laccase, ascorbate oxidase, and ceruloplasmin are the classical members of the multicopper oxidase family also known as blue oxidases. Recently, a small number of bacterial members of this family have been characterized, including CueO from E. coli a spore-coat laccase (CotA) from Bacillus suhtilis and phenoxazinone synthase from Streptomyces antibioticus The catalyzed reaction of these enzymes except for phenoxazinone synthase is given in Equation (11). A comprehensive overview of the broad and active research on blue copper oxidases is presented in Messerschmidt. Recent results have been included in a review on the reduction of dioxygen by copper-containing enzymes. The nature and number of the different copper sites in blue oxidases has been described in the sections about the type-1 copper site and the trinuclear copper cluster. 

Messerschmidt A. Blue copper oxidases. In Sykes AG (ed.), Advances in Inorganic Chemistry. Academic Press, San Diego, CA, 1993, pp. 121-185. 

Kroneck P. Redox properties of blue multi-copper oxidases. In Messerschmidt A (ed.), Multi-Copper Oxidases. World Scientific, Singapore, 1997, pp. 391-402. 

A Messerschmidt, A Rossi, R Ladenstein, R Huber, M Bolognesi, G Gatti, A Marchesini, R Petruzelli, A Finazzi-Agro. X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands. J Mol Biol 206 513-529, 1989. 

The similarity matrix calculated in Messerschmidt and Huber (202) indicates clearly the six-domain structure of ceruloplasmin and three-domain structures for laccase and ascorbate oxidase. The internal triplication within the ceruloplasmin amino-acid sequence is reflected by values of about 60% difference. Comparison of both the N-terminal domains and the C-terminal domains of the blue oxidases indicates, respectively, a relationship that is closer and relevant values for percent difference that are significantly lower than those for other comparisons. This might reflect the requirements for the trinuclear copper site. The lowest values of about 70 to 73% difference are observed for both N-terminal and C-terminal domains of laccase and ascorbate oxidase, showing that the two oxidases are more closely related to ceruloplasmin than either of them. 

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