Redox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude - Wikidata - awgldk - TriplyDB

Redox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude

Redox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude

http://www.wikidata.org/entity/Q58031620

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Protein design: toward functional metalloenzymes Design of a single protein that spans the entire 2-V range of physiological redox potentials Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Designed azurins show lower reorganization free energies for intraprotein electron transfer De novo-designed metallopeptides with type 2 copper centers: modulation of reduction potentials and nitrite reductase activities.Design of Heteronuclear Metalloenzymes.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers Hydrogen Bonds Dictate the Coordination Geometry of Copper: Characterization of a Square-Planar Copper(I) Complex.Prediction of Reduction Potentials of Copper Proteins with Continuum Electrostatics and Density Functional Theory.Stabilization of protein structure through π-π interaction in the second coordination sphere of pseudoazurin.

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Redox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude

http://www.wikidata.org/entity/Q58031620

description

im Januar 2012 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published on 22 March 2012

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована у 2012

@uk

name

Redox tuning of two biological ...... trend but different magnitude

@en

Redox tuning of two biological ...... trend but different magnitude

@nl

type

label

Redox tuning of two biological ...... trend but different magnitude

@en

Redox tuning of two biological ...... trend but different magnitude

@nl

prefLabel

Redox tuning of two biological ...... trend but different magnitude

@en

Redox tuning of two biological ...... trend but different magnitude

@nl

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Chemical Communications

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Redox tuning of two biological ...... trend but different magnitude

@en

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Feng Xue

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

Nicholas M Marshall

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

P2860

Structural basis of electron transfer modulation in the purple CuA center

How can a single second sphere amino acid substitution cause reduction midpoint potential changes of hundreds of millivolts?

Mechanism of CuA assembly

Pi-interaction tuning of the active site properties of metalloproteins

Rationally tuning the reduction potential of a single cupredoxin beyond the natural range

Solvent tuning of electrochemical potentials in the active sites of HiPIP versus ferredoxin.

Construction and characterization of an azurin analog for the purple copper site in cytochrome c oxidase

Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of MitoNEET: comparison to the (Cys)4 mutant and implications of the effects of pH on the labile metal center

Structures of metal sites of oxidized bovine heart cytochrome c oxidase at 2.8 A.

Copper coordination in blue proteins.

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4217-4219

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scholarly article

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10.1039/C2CC30901G

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35

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48

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2012-03-22T00:00:00Z

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22441412

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