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投稿者: Yuma Morimoto

Review

Copper Active Sites in Biology

Department of Chemistry, Stanford University, Stanford, California 94305, United States
Chem. Rev., Article ASAP
DOI: 10.1021/cr400327t
Publication Date (Web): March 3, 2014
Copyright © 2014 American Chemical Society
General Biochemistry

Table of Contents

  • 1. Introduction
  • 2. Electronic Structure and Spectroscopy
    • 2.1. Cu(I) Sites
      • 2.1.1. Cu(I) K-Edge XAS
      • 2.1.2. K-β Emission
    • 2.2. Mononuclear Cu(II) Sites
      • 2.2.1. Ligand Field Theory (LFT)
      • 2.2.2. Cu(II) Ground States
      • 2.2.3. Ligand Field Excited States
      • 2.2.4. Charge Transfer Excited States
      • 2.2.5. XAS K-Edge
      • 2.2.6. XAS L-Edge
      • 2.2.7. XMCD
    • 2.3. Binuclear Copper Sites
      • 2.3.1. Two Copper(II) Atoms: Magnetic Coupling
      • 2.3.2. Copper(II)–Copper(I)
    • 2.4. Higher Nuclearity Sites: Spin Frustration and Antisymmetric Exchange
    • 2.5. Electronic Structure Calculations
      • 2.5.1. Ab Initio Wave Function Methods
      • 2.5.2. Density Functional Methods
      • 2.5.3. Quantum Mechanics–Molecular Mechanics (QM–MM) Methods
      • 2.5.4. Application to Cu Sites
  • 3. Copper Active Sites That Activate Dioxygen
    • 3.1. Reversible O2 Binding: Overcoming the Spin-Forbiddenness
      • 3.1.1. Enzymology
      • 3.1.2. Thermodynamics and Kinetics
      • 3.1.3. Structure
      • 3.1.4. Electronic Structure
      • 3.1.5. Mechanism
    • 3.2. Oxygen Activation by Coupled Binuclear Active Sites: Polyphenol Oxidases and Phenol Oxygenases
      • 3.2.1. Enzymology
      • 3.2.2. Kinetics
      • 3.2.3. Structure
      • 3.2.4. Electronic Structure
      • 3.2.5. Mechanism
    • 3.3. O2 Activation for H-Atom Abstraction: Noncoupled Binuclear Copper Enzymes (Role of Exchange Coupling in Reactivity)
      • 3.3.1. Enzymology
      • 3.3.2. Kinetics
      • 3.3.3. Structure
      • 3.3.4. Electronic Structure and Spectroscopy
      • 3.3.5. Molecular Mechanism
      • 3.3.6. Exchange Coupling Contribution to Reactivity
    • 3.4. O2 Activation by a Mononuclear Cu Site: Cofactor Biogenesis in Galactose Oxidase
      • 3.4.1. Enzymology
      • 3.4.2. Kinetics
      • 3.4.3. Structure
      • 3.4.4. Electronic Structure
      • 3.4.5. Mechanism
    • 3.5. Particulate Methane Monooxygenase and Related Systems: H-Atom Abstraction from Methane
      • 3.5.1. Enzymology
      • 3.5.2. Kinetics
      • 3.5.3. Structure
      • 3.5.4. Electronic Structure
      • 3.5.5. Mechanism
    • 3.6. Structure/Function Correlations of O2 Activation by Copper Sites
    • 3.7. Structure/Function Correlations of O2 Reduction to H2O
      • 3.7.1. Multicopper Oxidases
      • 3.7.2. Heme–Copper Respiratory Oxidases
      • 3.7.3. Reduction of O2 to H2O
  • 4. Substrate Activation by Cu(II) Sites
    • 4.1. Quercetinase
      • 4.1.1. Enzymology
      • 4.1.2. Kinetics
      • 4.1.3. Structure
      • 4.1.4. Spectroscopy and Electronic Structure
      • 4.1.5. Molecular Mechanism
    • 4.2. Cofactor Biogenesis in the Copper Amine Oxidases
      • 4.2.1. Enzymology
      • 4.2.2. Kinetics
      • 4.2.3. Structure
      • 4.2.4. Spectroscopy and Electronic Structure
      • 4.2.5. Molecular Mechanism
    • 4.3. Nature of Cu(II) Substrate Activation
  • 5. Copper Sites in Bacterial Denitrification
    • 5.1. Copper Nitrite Reductase
    • 5.2. Nitrous Oxide Reductase
      • 5.2.1. Enzymology
      • 5.2.2. Kinetics
      • 5.2.3. Structure
      • 5.2.4. Spectroscopy and Electronic Structure
      • 5.2.5. Molecular Mechanism
  • 6. Concluding Comments
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