The type I copper center in multicopper oxidases is constructed from 1Cys2His and weakly coordinating 1Met or the non-coordinating 1Phe/1Leu, and it exhibits spectral properties and an alkaline transition similar to those of the blue copper center in blue copper proteins. Since the type I copper center in multicopper oxidases is deeply buried inside the protein molecule, electron transfers to and from type I copper are performed through specific pathways: the hydrogen bond between an amino acid located at the substrate binding site and a His residue coordinating type I copper, and the His-Cys-His sequence connecting the type I copper center and the trinuclear copper center comprised of a type II copper and a pair of type III coppers. The intramolecular electron transfer rates can be tuned by mutating the fourth ligand of type I copper. Further, mutation at the Cys ligand gives a vacant type I copper center and traps the reaction intermediate during the four-electron reduction of dioxygen.
Structure and function of type I copper in multicopper oxidases. Publishing Authors By Initials
Structure and function of type I copper in multicopper oxidases. Journal Published:
PUBLICATION TYPE: Research Support, Non-U.S. Gov
Journal: Cellular and molecular life sciences : CMLS
VOLUME: 64
Page Numbers: 2642-56
Journal Abbreviation: Cell. Mol. Life Sci.
ISSN: 1420-682X
DAY: 30
MONTH: Oct
YEAR: 2007
Structure and function of type I copper in multicopper oxidases. Information
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LANGUAGE: eng
NlmUniqueID: 9705402
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AFFILIATION: Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa, 920-1192, Japan. ts0513@kenroku.kanazawa-u.ac.jp
Country: Switzerland
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MEDLINETA: Cell Mol Life Sci
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