Metallo-oxidase Enzymes: Design of their Active Sites
AuthorXiao, Z; Wedd, AG
Source TitleAustralian Journal of Chemistry: an international journal for chemical science
Document TypeJournal Article
CitationsXiao, Z. & Wedd, A. G. (2011). Metallo-oxidase Enzymes: Design of their Active Sites. AUSTRALIAN JOURNAL OF CHEMISTRY, 64 (3), pp.231-238. https://doi.org/10.1071/CH10428.
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C1 - Journal Articles Refereed
Multi-copper oxidases are a large family of enzymes prevalent in all three domains of life. They couple the one-electron oxidation of substrate to the four-electron reduction of dioxygen to water and feature at least four Cu atoms, traditionally divided into three sites: T1, T2, and (binuclear) T3. The T1 site catalyzes substrate oxidation while a trinuclear cluster (comprising combined T2 and T3 centres) catalyzes the reduction of dioxygen. Substrate oxidation at the T1 Cu site occurs via an outer-sphere mechanism and consequently substrate specificities are determined primarily by the nature of a substrate docking/oxidation (SDO) site associated with the T1 Cu centre. Many of these enzymes ‘moonlight’, i.e. display broad specificities towards many different substrates and may have multiple cellular functions. A sub-set are robust catalysts for the oxidation of low-valent transition metal ions such as FeII, CuI, and MnII and are termed ‘metallo-oxidases’. They play essential roles in nutrient metal uptake and homeostasis, with the ferroxidase ceruloplasmin being a prominent member. Their SDO sites are tailored to facilitate specific binding and facile oxidation of these low-valent metal ions and this is the focus of this review.
KeywordsBioinorganic Chemistry; Expanding Knowledge in the Chemical Sciences
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