Protein control of true, gated, and coupled electron transfer reactions. - Wikidata - wikimedia - TriplyDB

Protein control of true, gated, and coupled electron transfer reactions.

Protein control of true, gated, and coupled electron transfer reactions.

http://www.wikidata.org/entity/Q30369100

about

Biochemistry and theory of proton-coupled electron transfer Mechanisms for control of biological electron transfer reactions Defining the Role of the Axial Ligand of the Type 1 Copper Site in Amicyanin by Replacement of Methionine with Leucine A joint x-ray and neutron study on amicyanin reveals the role of protein dynamics in electron transfer Proline 96 of the Copper Ligand Loop of Amicyanin Regulates Electron Transfer from Methylamine Dehydrogenase by Positioning Other Residues at the Protein−Protein Interface Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis Replacement of the axial copper ligand methionine with lysine in amicyanin converts it to a zinc-binding protein that no longer binds copper NADPH-cytochrome P450 oxidoreductase: prototypic member of the diflavin reductase family.Effects of interdomain tether length and flexibility on the kinetics of intramolecular electron transfer in human sulfite oxidase Fundamental signatures of short- and long-range electron transfer for the blue copper protein azurin at Au/SAM junctions Effect of solution viscosity on intraprotein electron transfer between the FMN and heme domains in inducible nitric oxide synthase Surface residues dynamically organize water bridges to enhance electron transfer between proteins.Faster interprotein electron transfer in a [myoglobin, b⁵] complex with a redesigned interface.Real-time analysis of conformational control in electron transfer reactions of human cytochrome P450 reductase with cytochrome c Characterization of the free energy dependence of an interprotein electron transfer reaction by variation of pH and site-directed mutagenesis.Designed azurins show lower reorganization free energies for intraprotein electron transfer Mechanism of protein oxidative damage that is coupled to long-range electron transfer to high-valent haems.Thermodynamic characterization of five key kinetic parameters that define neuronal nitric oxide synthase catalysis.Distance-independent charge recombination kinetics in cytochrome c-cytochrome c peroxidase complexes: compensating changes in the electronic coupling and reorganization energies Steering electrons on moving pathways.MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.A single residue controls electron transfer gating in photosynthetic reaction centers.Cupredoxins--a study of how proteins may evolve to use metals for bioenergetic processes.Gating mechanisms for biological electron transfer: integrating structure with biophysics reveals the nature of redox control in cytochrome P450 reductase and copper-dependent nitrite reductase.Kinetic and spectroscopic probes of motions and catalysis in the cytochrome P450 reductase family of enzymes.Orchestrated Domain Movement in Catalysis by Cytochrome P450 Reductase.A complete thermodynamic analysis of enzyme turnover links the free energy landscape to enzyme catalysis.Electron transfer within nitrogenase: evidence for a deficit-spending mechanism.Electrostatic redesign of the [myoglobin, cytochrome b5] interface to create a well-defined docked complex with rapid interprotein electron transfer Photoinitiated singlet and triplet electron transfer across a redesigned [myoglobin, cytochrome b5] interface.Characterization of electron tunneling and hole hopping reactions between different forms of MauG and methylamine dehydrogenase within a natural protein complex.Conformational gating of electron transfer from the nitrogenase Fe protein to MoFe protein.Exploring biological electron transfer pathway dynamics with the Pathways plugin for VMD.Single-electron self-exchange between cage hydrocarbons and their radical cations in the gas phase.Structural variability and dynamics of the P3HT/PCBM interface and its effects on the electronic structure and the charge-transfer rates in solar cells.Quantum effects in biological electron transfer

P2860

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P2860

Protein control of true, gated, and coupled electron transfer reactions.

http://www.wikidata.org/entity/Q30369100

description

2008 nî lūn-bûn

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2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

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2008年論文

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2008年论文

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name

Protein control of true, gated, and coupled electron transfer reactions.

@ast

Protein control of true, gated, and coupled electron transfer reactions.

@en

type

label

Protein control of true, gated, and coupled electron transfer reactions.

@ast

Protein control of true, gated, and coupled electron transfer reactions.

@en

prefLabel

Protein control of true, gated, and coupled electron transfer reactions.

@ast

Protein control of true, gated, and coupled electron transfer reactions.

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P1433

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Accounts of Chemical Research

P1476

Protein control of true, gated, and coupled electron transfer reactions

@en

P2093

Victor L Davidson

http://www.w3.org/2001/XMLSchema#string

P2860

MgATP-Bound and nucleotide-free structures of a nitrogenase protein complex between the Leu 127 Delta-Fe-protein and the MoFe-protein

Structure of the electron transfer complex between ferredoxin and ferredoxin-NADP(+) reductase

Mutation of alphaPhe55 of methylamine dehydrogenase alters the reorganization energy and electronic coupling for its electron transfer reaction with amicyanin

Extensive conformational sampling in a ternary electron transfer complex

Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c

Generation of novel copper sites by mutation of the axial ligand of amicyanin. Atomic resolution structures and spectroscopic properties

A single methionine residue dictates the kinetic mechanism of interprotein electron transfer from methylamine dehydrogenase to amicyanin

Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i

Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin

Tyr(30) of amicyanin is not critical for electron transfer to cytochrome c-551i: implications for predicting electron transfer pathways.

P304

730-738

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P31

scholarly article

P356

10.1021/AR700252C

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P433

6

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P478

41

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Victor L. Davidson

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2008-06-01T00:00:00Z

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18442271

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4860822

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