Structural basis of electron transfer modulation in the purple CuA center
about
Crystal structure of nitrous oxide reductase from Paracoccus denitrificans at 1.6 A resolutionProtein design: toward functional metalloenzymesComputational approaches for rational design of proteins with novel functionalitiesRole of the coordinating histidine in altering the mixed valency of Cu(A): an electron nuclear double resonance-electron paramagnetic resonance investigation.Design of functional metalloproteins.Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics.Binuclear Cu(A) Formation in Biosynthetic Models of Cu(A) in Azurin Proceeds via a Novel Cu(Cys)2His Mononuclear Copper Intermediate.The role of ligand-containing loops at copper sites in proteins.Electronic structure of the ground and excited states of the Cu(A) site by NMR spectroscopy.Axial interactions in the mixed-valent CuA active site and role of the axial methionine in electron transfer.pH-dependent transition between delocalized and trapped valence states of a CuA center and its possible role in proton-coupled electron transferMetalloproteins containing cytochrome, iron-sulfur, or copper redox centersMultiple forms of the catalytic centre, CuZ, in the enzyme nitrous oxide reductase from Paracoccus pantotrophus.Engineered lanthanide-binding metallohomeodomains: designing folded chimeras by modular turn substitution.Cleavage of the C-S bond with the formation of a binuclear copper complex with 2-thiolato-3-phenyl-5-(pyridine-2-ylmethylene)-3,5-dihydro-4H-imidazole-4-one. A new mimic of the active site of N2O reductase.An engineered CuA Amicyanin capable of intermolecular electron transfer reactions.Walking the seven lines: binuclear copper A in cytochrome c oxidase and nitrous oxide reductase.Probing the role of the backbone carbonyl interaction with the CuA center in azurin by replacing the peptide bond with an ester linkage.Native Cu(A) redox sites are largely resilient to pH variations within a physiological range.Characterization of a long overlooked copper protein from methane- and ammonia-oxidizing bacteriaRedox tuning of two biological copper centers through non-covalent interactions: same trend but different magnitude
P2860
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P2860
Structural basis of electron transfer modulation in the purple CuA center
description
1999 nî lūn-bûn
@nan
1999 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structural basis of electron transfer modulation in the purple CuA center
@ast
Structural basis of electron transfer modulation in the purple CuA center
@en
Structural basis of electron transfer modulation in the purple CuA center
@nl
type
label
Structural basis of electron transfer modulation in the purple CuA center
@ast
Structural basis of electron transfer modulation in the purple CuA center
@en
Structural basis of electron transfer modulation in the purple CuA center
@nl
prefLabel
Structural basis of electron transfer modulation in the purple CuA center
@ast
Structural basis of electron transfer modulation in the purple CuA center
@en
Structural basis of electron transfer modulation in the purple CuA center
@nl
P2093
P356
P1433
P1476
Structural basis of electron transfer modulation in the purple CuA center
@en
P2093
P304
P356
10.1021/BI9901634
P407
P577
1999-05-04T00:00:00Z