Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.

Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.

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http://www.wikidata.org/entity/Q33907362
Electronic Structure of a Cu(II)-Alkoxide Complex Modeling Intermediates in Copper-Catalyzed Alcohol OxidationsCorE from Myxococcus xanthus is a copper-dependent RNA polymerase sigma factor.The essential role of the Cu(II) state of Sco in the maturation of the Cu(A) center of cytochrome oxidase: evidence from H135Met and H135SeM variants of the Bacillus subtilis ScoThe lumenal loop Met672-Pro707 of copper-transporting ATPase ATP7A binds metals and facilitates copper release from the intramembrane sitesType 1 copper site synthetic model complexes with increased redox potentials.N-terminal region of CusB is sufficient for metal binding and metal transfer with the metallochaperone CusF.Design of a single protein that spans the entire 2-V range of physiological redox potentialsLumenal loop M672-P707 of the Menkes protein (ATP7A) transfers copper to peptidylglycine monooxygenase.Stable Cu(II) and Cu(I) mononuclear intermediates in the assembly of the CuA center of Thermus thermophilus cytochrome oxidase.Binuclear Cu(A) Formation in Biosynthetic Models of Cu(A) in Azurin Proceeds via a Novel Cu(Cys)2His Mononuclear Copper Intermediate.HHM motif at the CuH-site of peptidylglycine monooxygenase is a pH-dependent conformational switch.De novo design and characterization of copper metallopeptides inspired by native cupredoxins.Seeking the determinants of the elusive functions of Sco proteins.Morphological development and cytochrome c oxidase activity in Streptomyces lividans are dependent on the action of a copper bound Sco protein.Mono-nuclear copper complexes mimicking the intermediates for the binuclear copper center of the subunit II of cytochrome oxidase: a peptide based approach.The role of the Cys-X-X-X-Cys motif on the kinetics of cupric ion loading to the Streptomyces lividans Sco protein.Clarifying the Copper Coordination Environment in a de Novo Designed Red Copper Protein
P2860

Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.

Item
http://www.wikidata.org/entity/Q33907362
description
2010 nî lūn-bûn
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2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Anatomy of a red copper center ...... o and its Cys-to-Ala variants.
@ast
Anatomy of a red copper center ...... o and its Cys-to-Ala variants.
@en
type
label
Anatomy of a red copper center ...... o and its Cys-to-Ala variants.
@ast
Anatomy of a red copper center ...... o and its Cys-to-Ala variants.
@en
prefLabel
Anatomy of a red copper center ...... o and its Cys-to-Ala variants.
@ast
Anatomy of a red copper center ...... o and its Cys-to-Ala variants.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Anatomy of a red copper center ...... o and its Cys-to-Ala variants.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932