Activating Metal Sites for Biological Electron Transfer.
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E. Solomon | Ryan G. Hadt | Edward I Solomon | Benjamin E. R. Snyder | Ryan G Hadt | Benjamin E R Snyder
[1] K. Hodgson,et al. Resonant Inelastic X-ray Scattering on Ferrous and Ferric Bis-imidazole Porphyrin and Cytochrome c: Nature and Role of the Axial Methionine–Fe Bond , 2014, Journal of the American Chemical Society.
[2] S. I. Gorelsky,et al. Anisotropic Covalency Contributions to Superexchange Pathways in Type One Copper Active Sites , 2014, Journal of the American Chemical Society.
[3] Yi Lu,et al. Metalloproteins Containing Cytochrome, Iron–Sulfur, or Copper Redox Centers , 2014, Chemical reviews.
[4] Li Tian,et al. Copper active sites in biology. , 2014, Chemical reviews.
[5] Yi Lu,et al. Axial interactions in the mixed-valent CuA active site and role of the axial methionine in electron transfer , 2013, Proceedings of the National Academy of Sciences.
[6] K. Hodgson,et al. Spectroscopic and DFT studies of second-sphere variants of the type 1 copper site in azurin: covalent and nonlocal electrostatic contributions to reduction potentials. , 2012, Journal of the American Chemical Society.
[7] A. Dey,et al. Thermodynamic equilibrium between blue and green copper sites and the role of the protein in controlling function , 2009, Proceedings of the National Academy of Sciences.
[8] S. Elliott,et al. Methionine ligand lability of type I cytochromes c: detection of ligand loss using protein film voltammetry. , 2008, Journal of the American Chemical Society.
[9] E. Solomon,et al. Spectroscopic methods in bioinorganic chemistry: blue to green to red copper sites. , 2006, Inorganic chemistry.
[10] H. Marques,et al. The coordination of imidazole and substituted pyridines by the hemeoctapeptide N-acetyl-ferromicroperoxidase-8 (FeIINAcMP8). , 2004, Journal of inorganic biochemistry.
[11] D. Kosman,et al. Ferrous binding to the multicopper oxidases Saccharomyces cerevisiae Fet3p and human ceruloplasmin: contributions to ferroxidase activity. , 2004, Journal of the American Chemical Society.
[12] Robert K Szilagyi,et al. Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins. , 2004, Chemical reviews.
[13] G. Lushington,et al. Comparison of thioethers and sulfoxides as axial ligands for N-acetylmicroperoxidase-8: implications for oxidation of methionine-80 in cytochrome c. , 2003, Inorganic chemistry.
[14] E. Solomon,et al. Spectroscopic studies of the Met182Thr mutant of nitrite reductase: role of the axial ligand in the geometric and electronic structure of blue and green copper sites. , 2003, Journal of the American Chemical Society.
[15] K. Hodgson,et al. L-edge X-ray absorption spectroscopy of non-heme iron sites: experimental determination of differential orbital covalency. , 2003, Journal of the American Chemical Society.
[16] Harry B. Gray,et al. Copper coordination in blue proteins , 2000, JBIC Journal of Biological Inorganic Chemistry.
[17] P. A. Lay,et al. Determination of iron-ligand bond lengths in ferric and ferrous horse heart cytochrome c using multiple-scattering analyses of XAFS data , 1999 .
[18] H. Gray,et al. Effects of Ligation and Folding on Reduction Potentials of Heme Proteins , 1998 .
[19] Edward I. Solomon,et al. Spectroscopic and Geometric Variations in Perturbed Blue Copper Centers: Electronic Structures of Stellacyanin and Cucumber Basic Protein , 1998 .
[20] H. Gray,et al. Cytochrome c folding triggered by electron transfer. , 1996, Chemistry & biology.
[21] H. Gray,et al. Protein Folding Triggered by Electron Transfer , 1996, Science.
[22] R J Williams,et al. Energised (entatic) states of groups and of secondary structures in proteins and metalloproteins. , 1995, European journal of biochemistry.
[23] B. Malmström. Rack-induced bonding in blue-copper proteins. , 1994, European journal of biochemistry.
[24] 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 .
[25] 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 .
[26] 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.
[27] Edward I. Solomon,et al. ELECTRONIC STRUCTURES OF ACTIVE SITES IN COPPER PROTEINS : CONTRIBUTIONS TO REACTIVITY , 1992 .
[28] M. Newton,et al. Quantum chemical probes of electron-transfer kinetics: the nature of donor-acceptor interactions , 1991 .
[29] K. Hodgson,et al. X-ray absorption edge spectroscopy of ligands bound to open-shell metal ions: Chlorine K-edge studies of covalency in CuCl sub 4 sup 2 minus , 1990 .
[30] R. Huber,et al. X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands. , 1989, Journal of molecular biology.
[31] R. Marcus,et al. Electron transfers in chemistry and biology , 1985 .
[32] Edward I. Solomon,et al. Electronic structure and bonding of the blue copper site in plastocyanin , 1985 .
[33] J. Guss,et al. Structure of oxidized poplar plastocyanin at 1.6 A resolution. , 1983, Journal of molecular biology.
[34] Sebastian Doniach,et al. Observation of an electric quadrupole transition in the X-ray absorption spectrum of a Cu(II) complex , 1982 .
[35] E. Solomon,et al. Spectroscopic studies on plastocyanin single crystals: a detailed electronic structure determination of the blue copper active site , 1981 .
[36] B. Burgess,et al. Oxidation-reduction properties and complexation reactions of the iron-molybdenum cofactor of nitrogenase. , 1980, The Journal of biological chemistry.
[37] R. Hantgan,et al. Conformational dynamics in cytochrome c. A fragment exchange study. , 1978, The Journal of biological chemistry.
[38] M. Murata,et al. X-ray crystal structure analysis of plastocyanin at 2.7 Å resolution , 1978, Nature.
[39] H. Gray,et al. Spectroscopic studies and a structural model for blue copper centers in proteins. , 1976, Proceedings of the National Academy of Sciences of the United States of America.
[40] Gary J. Pielak,et al. Entropic Stabilization of Cytochrome c upon Reduction , 1995 .
[41] H B Gray,et al. Axial ligand replacement in horse heart cytochrome c by semisynthesis , 1989, Proteins.
[42] A. Gewirth,et al. Electronic structure of plastocyanin: excited state spectral features , 1988 .
[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] K. Hodgson,et al. Polarized x-ray absorption spectra of oriented plastocyanin single crystals. Investigation of methionine-copper coordination , 1982 .
[45] H. Schugar,et al. Preparation and Characterization of [rac-5, 7, 7, 12, 14, 14, -Hexamethyl-1, 4, 8, 11-Tetraazocyclotetradecane]Copper(II) o-Mercaptobenzoate Hydrate, [Cu(tet b)(o-SC6H4CO2)].H2O, a Complex with a CuN4S (Mercaptide) Chromophore , 1979 .