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2000, Journal of Biological Inorganic Chemistry
centers are summarized and their relation to intra- and inter-protein electron transfer (ET) kinetics are described. Specific contributions of the electronic structures of these two broad classes of Cu ET proteins to H AB, λ, and Δ E° are discussed. Also, the role of the protein structure in determining key geometric features which define the electronic structures of the metal sites in these proteins is considered.
Advanced Science
Electron Transfer Proteins as Electronic Conductors: Significance of the Metal and Its Binding Site in the Blue Cu Protein, Azurin2015 •
Journal of the American Chemical Society
Spectroscopy of Mixed-Valence Cu A -Type Centers: Ligand-Field Control of Ground-State Properties Related to Electron Transfer1998 •
Current Opinion in Chemical Biology
Electronic structure and its relation to function in copper proteins2002 •
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.
Theoretical and Experimental Chemistry
Kinetics of outer-sphere electron transfer reactions involving synthetic models of copper ?blue"? proteins1994 •
Pure and Applied Chemistry
Electronic structure contributions to function in bioorganic chemistry: The blue copper active site1998 •
Inorganica Chimica Acta
Electronic structure of the oxidized and reduced blue copper sites: contributions to the electron transfer pathway, reduction potential, and geometry1996 •
1985 •
Inorganica Chimica Acta
Tunneling matrix element in Ru-modified blue copper proteins: pruning the protein in search of electron transfer pathways1996 •
Proceedings of the National Academy of Sciences
Marked changes in electron transport through the blue copper protein azurin in the solid state upon deuteration2012 •
Measuring solid-state electron transport (ETp) across proteins allows studying electron transfer (ET) mechanism(s), while minimizing solvation effects on the process. ETp is, however, sensitive to any static (conformational) or dynamic (vibrational) changes in the protein. Our macroscopic measurements allow extending ETp studies to low temperatures, with the concomitant resolution of lower current densities, because of the larger electrode contact areas. Thus, earlier we reported temperature-independent ETp via the copper protein azurin (Az), from 80 K until denaturation, whereas for apo-Az ETp was temperature dependent above 180 K. Deuteration (H/D substitution) may provide mechanistic information on the question of whether the ETp involves H-bonds in the solid state. Here we report results of kinetic deuterium isotope effect (KIE) measurements on ETp through holo-Az as a function of temperature (30–340 K). Strikingly, deuteration changed ETp from temperature independent to tempera...
Protein Science - PROTEIN SCI
Quantum chemical calculations of the reorganization energy of blue-copper proteins1998 •
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Journal of The American Chemical Society
Resonance Raman excitation profiles indicate multiple Cys .fwdarw. Cu charge transfer transitions in type 1 copper proteins1993 •
Inorganic …
A Structural Strategy for Generating Rapid Electron-Transfer Kinetics in Copper (II/I) Systems1999 •
The Journal of Chemical Physics
The axial methionine ligand may control the redox reorganizations in the active site of blue copper proteins2010 •
Springer eBooks
Electronic Structures of Active Sites in Copper Proteins: Coupled Binuclear and Trinuclear Cluster Sites1993 •
2002 •
Chemical Society Reviews
Mixed valent sites in biological electron transfer2008 •
Journal of the American Chemical Society
Comparative ENDOR study of six blue copper proteins1984 •
Proceedings of the …
Fundamental signatures of short-and long-range electron transfer for the blue copper protein azurin at Au/SAM junctions2010 •
Journal of The American Chemical Society
A Quantitative Description of the Ground-State Wave Function of Cu A by X-ray Absorption Spectroscopy: Comparison to Plastocyanin and Relevance to Electron Transfer2001 •
Biosensors and Bioelectronics
Direct electron transfer between copper-containing proteins and electrodes2005 •
Electrochemistry Communications
Electrochemical and spectral characterization of blue copper protein models2009 •
The journal of physical chemistry. A
Electronic and Photophysical Properties of [Re (L)(CO)3(phen)](+) and [Ru(L)2(bpy)2](2+) (L = imidazole), Building Units for Long-Range Electron Transfer in Modified Blue Copper Proteins2016 •
Science Reviews - from the end of the world
Modulation of Functional Features in Electron Transferring Metalloproteins2020 •
Journal of The American Chemical Society
Role of the Surface-Exposed and Copper-Coordinating Histidine in Blue Copper Proteins: The Electron-Transfer and Redox-Coupled Ligand Binding Properties of His117Gly Azurin2000 •
Journal of the …
Spectroscopic and Electronic Structural Studies of Blue Copper Model Complexes. 1. Perturbation of the Thiolate−Cu Bond2000 •
European Journal of Biochemistry
The effect of driving force on intramolecular electron transfer in proteins. Studies on single-site mutated azurins1992 •
Journal of the American Chemical Society
Dramatic Electronic Perturbations of CuA Centers via Subtle Geometric Changes2019 •
The Journal of Physical Chemistry
Electron-transfer reactions in proteins: A calculation of electronic coupling1990 •
2003 •
Inorganica Chimica Acta
Complexes of CuII with mixed-donor phenanthroline-containing macrocycles: analysis of their structural, redox and spectral properties in the context of Type-1 blue copper proteins biomimetic models2005 •
2001 •