Abstract
Many metalloenzymes exhibit distinctive spectral features that are now becoming well understood. These reflect active site electronic structures that can make significant contributions to catalysis. Copper proteins provide well-characterized examples in which the unusual electronic structures of their active sites contribute to rapid, long-range electron transfer reactivity, oxygen binding and activation, and the multielectron reduction of dioxygen to water.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Copper / analysis
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Copper / metabolism
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Electron Spin Resonance Spectroscopy
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Electron Transport
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Enzymes / chemistry*
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Enzymes / metabolism
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Hemocyanins / chemistry
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Hemocyanins / metabolism
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Metalloproteins / chemistry*
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Metalloproteins / metabolism
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Models, Molecular
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Plastocyanin / chemistry
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Plastocyanin / metabolism
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Protein Conformation*
Substances
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Enzymes
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Metalloproteins
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Copper
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Hemocyanins
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Plastocyanin