Reversible Cleavage and Formation of the Dioxygen O-O Bond Within a Dicopper Complex

A key step in dioxygen evolution during photosynthesis is the oxidative generation of the O-O bond from water by a manganese cluster consisting of M2(μ-O)2 units (where M is manganese). The reverse reaction, reductive cleavage of the dioxygen O-O bond, is performed at a variety of dicopper and di-iron active sites in enzymes that catalyze important organic oxidations. Both processes can be envisioned to involve the interconversion of dimetal-dioxygen adducts, M2(O2), and isomers having M2(μ-O)2 cores. The viability of this notion has been demonstrated by the identification of an equilibrium between synthetic complexes having [Cu2(μ-η2:η2-O2)]2+ and [Cu2(μ-O)2]2+ cores through kinetic, spectroscopic, and crystallographic studies.

[1]  K. Karlin,et al.  Kinetic, thermodynamic, and spectral characterization of the primary copper-oxygen (Cu-O2) adduct in a reversibly formed and structurally characterized peroxo-dicopper(II) complex , 1991 .

[2]  E. C. Wilkinson,et al.  Modeling Copper-Dioxygen Reactivity in Proteins: Aliphatic C-H Bond Activation by a New Dicopper(II)-Peroxo Complex , 1994 .

[3]  Jason A. Halfen,et al.  Structural Characterization of the First Example of a Bis(μ-thiolato)dicopper(II) Complex, Relevance to Proposals for the Electron Transfer Sites in Cytochrome c Oxidase and Nitrous Oxide Reductase , 1995 .

[4]  E. C. Wilkinson,et al.  A HIGH-VALENT NONHEME IRON INTERMEDIATE. STRUCTURE AND PROPERTIES OF FE2(MU -O)2(5-ME-TPA)2(CLO4)3 , 1995 .

[5]  T. Meyer,et al.  Water oxidation by [(bpy)2(O)RuVORuV(O)(bpy)2] 4+. An oxygen-labeling study , 1990 .

[6]  Interaction of Manganese with Dioxygen and Its Reduced Derivatives , 1994 .

[7]  R. H. Holm,et al.  Fluoride-bridged dimers : binuclear copper(II) complexes and iron(III)-copper(II) assemblies , 1993 .

[8]  E. C. Wilkinson,et al.  A New Intermediate in Copper Dioxygen Chemistry: Breaking the O-O Bond To Form a {Cu2(.mu.-O)2}2+ Core , 1995 .

[9]  L. Que,et al.  The First Bis(.mu.-oxo)diiron(III) Complex. Structure and Magnetic Properties of [Fe2(.mu.-O)2(6TLA)2](ClO4)2 , 1995 .

[10]  V. DeRose,et al.  Where plants make oxygen: a structural model for the photosynthetic oxygen-evolving manganese cluster , 1993 .

[11]  J. Bollinger,et al.  Mechanism of Assembly of the Tyrosyl Radical-Diiron(III) Cofactorof E. coli Ribonucleotide Reductase. 3. Kinetics of the Limiting Fe2+ Reaction by Optical, EPR, and Moessbauer Spectroscopies , 1994 .

[12]  Stephen J. Lippard,et al.  Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane , 1993, Nature.

[13]  C. Mcauliffe,et al.  Synthesis of a bis-manganese water splitting complex , 1994 .

[14]  R. Ramaraj,et al.  Oxygen Evolution by Water Oxidation Mediated by Heterogeneous Manganese Complexes , 1986 .

[15]  Edward I. Solomon,et al.  ELECTRONIC STRUCTURES OF ACTIVE SITES IN COPPER PROTEINS : CONTRIBUTIONS TO REACTIVITY , 1992 .

[16]  Susan W. Gersten,et al.  Structure and redox properties of the water-oxidation catalyst [(bpy)2(OH2)RuORu(OH2)(bpy)2]4+ , 1985 .

[17]  Andrew L. Feig,et al.  Reactions of Non-Heme Iron(II) Centers with Dioxygen in Biology and Chemistry , 1994 .

[18]  Y. Naruta,et al.  Oxygen Evolution by Oxidation of Water with Manganese Porphyrin Dimers , 1994 .

[19]  J. Lipscomb,et al.  Transient intermediates of the methane monooxygenase catalytic cycle. , 1993, The Journal of biological chemistry.

[20]  Karl Wieghardt,et al.  The Active Sites in Manganese‐Containing Metalloproteins and Inorganic Model Complexes , 1989 .

[21]  L. Que,et al.  Dinuclear iron- and manganese-oxo sites in biology , 2007 .

[22]  Klaus H. Theopold,et al.  HYDROGEN TUNNELING IN THE ACTIVATION OF DIOXYGEN BY A TRIS(PYRAZOLYL)BORATE COBALT COMPLEX , 1994 .

[23]  B. Fox,et al.  A Transient Intermediate of the Methane Monooxygenase Catalytic Cycle Containing an FeIVFeIV Cluster , 1993 .

[24]  R. Hoffmann,et al.  Molecular Mechanism of Photosynthetic Oxygen Evolution. A Theoretical Approach , 1992 .

[25]  Akira Nakamura,et al.  A new model for dioxygen binding in hemocyanin. Synthesis, characterization, and molecular structure of the .mu.-.eta.2:.eta.2 peroxo dinuclear copper(II) complexes, [Cu(HB(3,5-R2pz)3)]2(O2) (R = isopropyl and Ph) , 1992 .

[26]  D. Root,et al.  Spectroscopy of Binuclear Dioxygen Complexes , 1994 .

[27]  K. Karlin,et al.  Kinetics and thermodynamics of formation of copper-dioxygen adducts: oxygenation of mononuclear copper(I) complexes containing tripodal tetradentate ligands , 1993 .

[28]  Bart Hazes,et al.  Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences , 1994, Proteins.

[29]  J N Rodríguez-López,et al.  Tyrosinase: a comprehensive review of its mechanism. , 1995, Biochimica et biophysica acta.

[30]  Hans Eklund,et al.  Three-dimensional structure of the free radical protein of ribonucleotide reductase , 1990, Nature.

[31]  K. Karlin,et al.  Dioxygen-copper reactivity ― models for hemocyanin: reversible O2 and CO binding to structurally characterized dicopper(I) complexes containing hydrocarbon-linked bis[2-(2-pyridyl)ethyl]amine units , 1988 .

[32]  Thomas G. Spiro,et al.  Characterization of a Diiron(III) Peroxide Intermediate in the Reaction Cycle of Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath) , 1995 .

[33]  Athanasios Salifoglou,et al.  Spectroscopic detection of intermediates in the reaction of dioxygen with the reduced methane monooxygenase/hydroxylase from Methylococcus capsulatus (Bath) , 1994 .

[34]  H. Eklund,et al.  Structure and function of the Escherichia coli ribonucleotide reductase protein R2. , 1993, Journal of molecular biology.