A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase.
about
The STRING database in 2011: functional interaction networks of proteins, globally integrated and scoredTraditional biomolecular structure determination by NMR spectroscopy allows for major errors.Unusual Cu(I)/Ag(I) coordination ofEscherichia coliCusF as revealed by atomic resolution crystallography and X-ray absorption spectroscopyCu(I) recognition via cation-π and methionine interactions in CusFMechanism of CuA assemblySco proteins are involved in electron transfer processesA new structural paradigm in copper resistance in Streptococcus pneumoniaeStructural and mechanistic insights into an extracytoplasmic copper trafficking pathway in Streptomyces lividansThe CopC Family: Structural and Bioinformatic Insights into a Diverse Group of Periplasmic Copper Binding ProteinsCopper metallochaperonesCopper control of bacterial nitrous oxide emission and its impact on vitamin B12-dependent metabolismThe roles of Rhodobacter sphaeroides copper chaperones PCu(A)C and Sco (PrrC) in the assembly of the copper centers of the aa(3)-type and the cbb(3)-type cytochrome c oxidasesA place for thioether chemistry in cellular copper ion recognition and trafficking.Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transfer.Stable Cu(II) and Cu(I) mononuclear intermediates in the assembly of the CuA center of Thermus thermophilus cytochrome oxidase.Cooperation between two periplasmic copper chaperones is required for full activity of the cbb3 -type cytochrome c oxidase and copper homeostasis in Rhodobacter capsulatus.Seeking the determinants of the elusive functions of Sco proteins.Biogenesis of cbb(3)-type cytochrome c oxidase in Rhodobacter capsulatusMutagenic analysis of Cox11 of Rhodobacter sphaeroides: insights into the assembly of Cu(B) of cytochrome c oxidase.The ScoI homologue SenC is a copper binding protein that interacts directly with the cbb₃-type cytochrome oxidase in Rhodobacter capsulatus.Copper trafficking in biology: an NMR approach.Analysis of copper-ligand bond lengths in X-ray structures of different types of copper sites in proteins.Functional analysis of the copy 1 of the fixNOQP operon of Ensifer meliloti under free-living micro-oxic and symbiotic conditions.The role of the Cys-X-X-X-Cys motif on the kinetics of cupric ion loading to the Streptomyces lividans Sco protein.The extracytoplasmic function σ factor σ(C) regulates expression of a branched quinol oxidation pathway in Corynebacterium glutamicum.Widespread Distribution and Functional Specificity of the Copper Importer CcoA: Distinct Cu Uptake Routes for Bacterial Cytochrome c Oxidases.A Copper Relay System Involving Two Periplasmic Chaperones Drives cbb3-Type Cytochrome c Oxidase Biogenesis in Rhodobacter capsulatus.
P2860
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P2860
A copper(I) protein possibly involved in the assembly of CuA center of bacterial cytochrome c oxidase.
description
2005 nî lūn-bûn
@nan
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մարտին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
A copper(I) protein possibly i ...... acterial cytochrome c oxidase.
@ast
A copper(I) protein possibly i ...... acterial cytochrome c oxidase.
@en
type
label
A copper(I) protein possibly i ...... acterial cytochrome c oxidase.
@ast
A copper(I) protein possibly i ...... acterial cytochrome c oxidase.
@en
prefLabel
A copper(I) protein possibly i ...... acterial cytochrome c oxidase.
@ast
A copper(I) protein possibly i ...... acterial cytochrome c oxidase.
@en
P2093
P2860
P50
P356
P1476
A copper(I) protein possibly i ...... acterial cytochrome c oxidase.
@en
P2093
Efthalia Katsari
Karel Kubicek
Nikolaos Katsaros
Stefano Mangani
P2860
P304
P356
10.1073/PNAS.0406150102
P407
P577
2005-03-07T00:00:00Z