Electronic structure contributions to function in bioinorganic chemistry.
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.
Department of Chemistry, Stanford University, CA 94305.
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Solomon
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Lowery
D000595:Amino Acid Sequence; D003300:Copper / Q000032:analysis / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D006433:Hemocyanins / Q000737:chemistry / Q000378:metabolism; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D010970:Plastocyanin / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation
D004798:Enzymes; D008667:Metalloproteins; D003300:Copper; D006433:Hemocyanins; D010970:Plastocyanin