Spectroscopic and DFT studies of second-sphere variants of the type 1 copper site in azurin: covalent and nonlocal electrostatic contributions to reduction potentials.
about
Protein design: toward functional metalloenzymesCopper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurinCopper active sites in biologyPicosecond sulfur K-edge X-ray absorption spectroscopy with applications to excited state proton transferMechanism of the reduction of the native intermediate in the multicopper oxidases: insights into rapid intramolecular electron transfer in turnover.Electron transfer and reaction mechanism of laccasesDesign of a single protein that spans the entire 2-V range of physiological redox potentialsDesign and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Design of Heteronuclear Metalloenzymes.Assessment of Quantum Mechanical Methods for Copper and Iron Complexes by Photoelectron Spectroscopy.Modulating the Copper-Sulfur Interaction in Type 1 Blue Copper Azurin by Replacing Cys112 with Nonproteinogenic Homocysteine.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centersSulfur K-Edge XAS Studies of the Effect of DNA Binding on the [Fe4S4] Site in EndoIII and MutY.A general method for artificial metalloenzyme formation through strain-promoted azide-alkyne cycloaddition.Activating Metal Sites for Biological Electron Transfer.Anisotropic covalency contributions to superexchange pathways in type one copper active sites.Prediction of Reduction Potentials of Copper Proteins with Continuum Electrostatics and Density Functional Theory.Copper Oxidation/Reduction in Water and Protein: Studies with DFTB3/MM and VALBOND Molecular Dynamics Simulations.A few key residues determine the high redox potential shift in azurin mutants.Fluctuating hydrogen-bond networks govern anomalous electron transfer kinetics in a blue copper protein.Control of the Electronic Ground State on an Electron-Transfer Copper Site by Second-Sphere Perturbations
P2860
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P2860
Spectroscopic and DFT studies of second-sphere variants of the type 1 copper site in azurin: covalent and nonlocal electrostatic contributions to reduction potentials.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Spectroscopic and DFT studies ...... tions to reduction potentials.
@ast
Spectroscopic and DFT studies ...... tions to reduction potentials.
@en
type
label
Spectroscopic and DFT studies ...... tions to reduction potentials.
@ast
Spectroscopic and DFT studies ...... tions to reduction potentials.
@en
prefLabel
Spectroscopic and DFT studies ...... tions to reduction potentials.
@ast
Spectroscopic and DFT studies ...... tions to reduction potentials.
@en
P2093
P2860
P356
P1476
Spectroscopic and DFT studies ...... tions to reduction potentials.
@en
P2093
Britt Hedman
Keith O Hodgson
Nicholas M Marshall
Ryan G Hadt
P2860
P304
16701-16716
P356
10.1021/JA306438N
P407
P577
2012-10-02T00:00:00Z