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- W1577659006 abstract "Abstract The copper enzymes covered in this article span a wide range in terms of both their structural and reactivity properties. Yet the copper centers in each share similar coordination geometries and have been designated ‘Type 2 (or II)’ copper proteins. Type 2 copper proteins lack the unique spectroscopic or magnetic signatures that typify the so‐called Type 1 and Type 3 copper proteins, and the unique tetranuclear cluster found in nitrous oxide reductase. Indeed, the basis for classifying proteins as Type 2 was that the EPR (Electron Paramagnetic Resonance) spectra of the oxidized (resting) forms of these proteins closely resembled the spectra of ‘normal’ tetragonal Cu II complexes, with g ∥ > g ⊥ > 2.00, and A ∥ ≥ 120 G at X‐band. It was generally surmised that the coordination environments of the copper sites in such enzymes were unexceptional, with five‐ or six‐coordinate structures composed of N, O ligands. As is often the case in science, many fascinating and totally unexpected structural and chemical phenomena turned out to be concealed behind this deceptively ‘normal’ facade. Each of the Type 2 enzymes covered here (superoxide dismutase, amine oxidase, lysyl oxidase, galactose oxidase, dopamine‐β‐monooxygenase, peptidylglycine α‐hydroxylating monooxygenase, and quercetinase) displays unique active‐site properties. Elucidating and elaborating structure/function relationships for these enzymes has been greatly aided by the availability of high‐resolution crystal structures for one or more enzymes from each group. These have generally corroborated the fairly detailed structural models that were developed from extensive spectroscopic studies. At the same time, the 3D structures have revealed many surprising details of the active sites. Indeed, the roles of copper in these ‘normal’ Type 2 copper centers are more diverse than ever imagined." @default.
- W1577659006 created "2016-06-24" @default.
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- W1577659006 date "2005-09-07" @default.
- W1577659006 modified "2023-10-03" @default.
- W1577659006 title "Copper Proteins with Type 2 Sites" @default.
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- W1577659006 doi "https://doi.org/10.1002/9781119951438.eibc0274" @default.
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