Electronic structure and its relation to function in copper proteins.

Spectroscopic and theoretical investigations of the geometric and electronic structures of mononuclear and binuclear copper sites in proteins help in understanding the contributions of these proteins to biological electron transfer. Spectroscopically calibrated density functional theory calculations, which give reasonable bonding descriptions in both ground- and excited-states, define the role of the protein in determining the geometric and electronic structure of the active site.

[1]  T. Tomizaki,et al.  Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A , 1995, Science.

[2]  A. Sykes.  Plastocyanin and the Blue Copper Proteins , 1990 .

[3]  E. Solomon,et al.  Spectroscopic Calibration of Modern Density Functional Methods Using [CuCl4]2- , 2002 .

[4]  Susan L. Cohen,et al.  Spectroscopic and Theoretical Studies of the Unusual EPR Parameters of Distorted Tetrahedral Cupric Sites:' Correlations to X-ray Spectral Features of Core Levels , 1987 .

[5]  K. Hodgson,et al.  Electronic structure description of the mu(4)-sulfide bridged tetranuclear Cu(Z) center in N(2)O reductase. , 2002, Journal of the American Chemical Society.

[6]  H. Bartunik,et al.  Accuracy and precision in protein structure analysis: restrained least-squares refinement of the structure of poplar plastocyanin at 1.33 A resolution. , 1992, Acta crystallographica. Section B, Structural science.

[7]  Björn O. Roos,et al.  A theoretical study of the copper–cysteine bond in blue copper proteins , 2001 .

[8]  E. Solomon,et al.  ELECTRONIC STRUCTURE OF THE REDUCED BLUE COPPER ACTIVE SITE : CONTRIBUTIONS TO REDUCTION POTENTIALS AND GEOMETRY , 1995 .

[9]  Edward I. Solomon,et al.  Spectroscopic and Electronic Structural Studies of Blue Copper Model Complexes. 1. Perturbation of the Thiolate−Cu Bond , 2000 .

[10]  Axel D. Becke,et al.  Density‐functional thermochemistry. IV. A new dynamical correlation functional and implications for exact‐exchange mixing , 1996 .

[11]  Björn O. Roos,et al.  Relation between the Structure and Spectroscopic Properties of Blue Copper Proteins , 1998 .

[12]  Peter Comba,et al.  Coordination compounds in the entatic state , 2000 .

[13]  Yi Lu,et al.  Spectroscopy of Mixed-Valence CuA-Type Centers: Ligand-Field Control of Ground-State Properties Related to Electron Transfer , 1998 .

[14]  K. Hodgson,et al.  Electronic structure of the perturbed blue copper site in nitrite reductase: spectroscopic properties, bonding and implications for the entatic/rack state. , 1996 .

[15]  A. Palmer,et al.  Oxygen Binding, Activation, and Reduction to Water by Copper Proteins. , 2001, Angewandte Chemie.

[16]  Edward I. Solomon,et al.  Spectroscopic and Geometric Variations in Perturbed Blue Copper Centers: Electronic Structures of Stellacyanin and Cucumber Basic Protein , 1998 .

[17]  U. Ryde,et al.  The structure and function of blue copper proteins , 2001 .

[18]  A. Gewirth,et al.  Electronic structure of plastocyanin: excited state spectral features , 1988 .

[19]  R J Williams,et al.  Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. , 1995, European journal of biochemistry.

[20]  J. Godden,et al.  The Structure of Copper-nitrite Reductase from Achromobacter cycloclastes at Five pH Values, with NO−2 Bound and with Type II Copper Depleted (*) , 1995, The Journal of Biological Chemistry.

[21]  B. Malmström.  Rack-induced bonding in blue-copper proteins. , 1994, European journal of biochemistry.

[22]  U. Ryde,et al.  Protein strain in blue copper proteins studied by free energy perturbations , 1999, Proteins.

[23]  Hartmut Michel,et al.  Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans , 1995, Nature.

[24]  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 .

[25]  Harry B. Gray,et al.  Copper coordination in blue proteins , 2000, JBIC Journal of Biological Inorganic Chemistry.

[26]  B. Hoffman,et al.  Ligand spin densities in blue copper proteins by q-band proton and nitrogen-14 ENDOR spectroscopy , 1991 .

[27]  K. Hodgson,et al.  Ligand K-edge X-ray absorption spectroscopy: a direct probe of ligand-metal covalency. , 2000, Accounts of chemical research.

[28]  Ulf Ryde,et al.  A comparison of the inner-sphere reorganization energies of cytochromes, iron-sulphur clusters, and blue copper proteins , 2001 .

[29]  N. Lehnert,et al.  Recent advances in bioinorganic spectroscopy. , 2001, Current opinion in chemical biology.

[30]  U. Ryde,et al.  Geometry, reduction potential, and reorganization energy of the binuclear Cu(A) site, studied by density functional theory. , 2001, Journal of the American Chemical Society.

[31]  Edward I. Solomon,et al.  Spectroscopic and Electronic Structural Studies of Blue Copper Model Complexes. 2. Comparison of Three- and Four-Coordinate Cu(II)−Thiolate Complexes and Fungal Laccase , 2000 .

[32]  Ulf Ryde,et al.  Structure, strain, and reorganization energy of blue copper models in the protein , 2001 .

[33]  I. Bertini,et al.  High-Field NMR Studies of Oxidized Blue Copper Proteins: The Case of Spinach Plastocyanin , 1999 .

[34]  K. Hodgson,et al.  X-ray Absorption Edge and EXAFS Studies of the Blue Copper Site in Stellacyanin: Effects of Axial Amide Coordination† , 2000 .

[35]  Peter Comba,et al.  Hybrid quantum mechanics/molecular mechanics studies of the active site of the blue copper proteins amicyanin and rusticyanin , 2001 .

[36]  A. Wang,et al.  Structural basis of electron transfer modulation in the purple CuA center. , 1999, Biochemistry.

[37]  Edward I. Solomon,et al.  X-ray absorption spectroscopic studies of the blue copper site: Metal and ligand K-edge studies to probe the origin of the EPR hyperfine splitting in plastocyanin , 1993 .

[38]  Wolfram Koch,et al.  A Chemist's Guide to Density Functional Theory , 2000 .

[39]  Björn O. Roos,et al.  On the role of strain in blue copper proteins , 2000, JBIC Journal of Biological Inorganic Chemistry.

[40]  E. Solomon,et al.  Electronic structures of active sites in electron transfer metalloproteins: contributions to reactivity , 2000 .

[41]  B. Roos,et al.  The cupric geometry of blue copper proteins is not strained. , 1996, Journal of molecular biology.

[42]  Feng Xu,et al.  Spectroscopic Studies and Electronic Structure Description of the High Potential Type 1 Copper Site in Fungal Laccase: Insight into the Effect of the Axial Ligand , 1999 .

[43]  Stephen V. Didziulis,et al.  Variable photon energy photoelectron spectroscopic studies of copper chlorides: an experimental probe of metal-ligand bonding and changes in electronic structure on ionization , 1988 .

[44]  H. Gray,et al.  On the Relationship between Protein-Forced Ligand Fields and the Properties of Blue Copper Centers , 1983 .

[45]  D. Kastrau,et al.  Multifrequency EPR evidence for a bimetallic center at the CuA site in cytochrome c oxidase , 1990, FEBS letters.

[46]  E. Solomon,et al.  Copper L-edge spectral studies. A direct experimental probe of the ground-state covalency in the blue copper site in plastocyanin , 1993 .

[47]  Edward I. Solomon,et al.  Electronic structure and bonding of the blue copper site in plastocyanin , 1985 .

[48]  K. Hodgson,et al.  A quantitative description of the ground-state wave function of Cu(A) by X-ray absorption spectroscopy: comparison to plastocyanin and relevance to electron transfer. , 2001, Journal of the American Chemical Society.