Redox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude
about
Protein design: toward functional metalloenzymesDesign 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.Designed azurins show lower reorganization free energies for intraprotein electron transferDe 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 centersHydrogen 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
description
im Januar 2012 veröffentlichter wissenschaftlicher Artikel
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scientific article published on 22 March 2012
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wetenschappelijk artikel
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наукова стаття, опублікована у 2012
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name
Redox tuning of two biological ...... trend but different magnitude
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Redox tuning of two biological ...... trend but different magnitude
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type
label
Redox tuning of two biological ...... trend but different magnitude
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Redox tuning of two biological ...... trend but different magnitude
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prefLabel
Redox tuning of two biological ...... trend but different magnitude
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Redox tuning of two biological ...... trend but different magnitude
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P1476
Redox tuning of two biological ...... trend but different magnitude
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Nicholas M Marshall
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10.1039/C2CC30901G
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P577
2012-03-22T00:00:00Z