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RESEARCH FRONT
Contents Vol 64(3)

Metallo-oxidase Enzymes: Design of their Active Sites*

Zhiguang Xiao A B and Anthony G. Wedd A B
+ Author Affiliations
- Author Affiliations

A School of Chemistry and Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Vic. 3010, Australia.

B Corresponding authors. Email: z.xiao@unimelb.edu.au, agw@unimelb.edu.au




Zhiguang Xiao (left) is a Research Fellow and Anthony G. Wedd (right) is a Professorial Fellow in the Bio21 Molecular Science and Biotechnology Research Institute and School of Chemistry at the University of Melbourne, Australia.

Australian Journal of Chemistry 64(3) 231-238 https://doi.org/10.1071/CH10428
Submitted: 25 November 2010  Accepted: 17 January 2011   Published: 11 March 2011

Abstract

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.


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