Controlling the chiral inversion reaction of the metallopeptide Ni-asparagine-cysteine-cysteine with dioxygen. - Wikidata - awgldk - TriplyDB

Controlling the chiral inversion reaction of the metallopeptide Ni-asparagine-cysteine-cysteine with dioxygen.

Controlling the chiral inversion reaction of the metallopeptide Ni-asparagine-cysteine-cysteine with dioxygen.

http://www.wikidata.org/entity/Q37612402

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Accessing Ni(III)-thiolate versus Ni(II)-thiyl bonding in a family of Ni-N2S2 synthetic models of NiSOD Embedding the Ni-SOD mimetic Ni-NCC within a polypeptide sequence alters the specificity of the reaction pathway.

P2860

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P2860

Controlling the chiral inversion reaction of the metallopeptide Ni-asparagine-cysteine-cysteine with dioxygen.

http://www.wikidata.org/entity/Q37612402

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 28 August 2012

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Controlling the chiral inversi ...... steine-cysteine with dioxygen.

@en

Controlling the chiral inversi ...... steine-cysteine with dioxygen.

@nl

type

label

Controlling the chiral inversi ...... steine-cysteine with dioxygen.

@en

Controlling the chiral inversi ...... steine-cysteine with dioxygen.

@nl

prefLabel

Controlling the chiral inversi ...... steine-cysteine with dioxygen.

@en

Controlling the chiral inversi ...... steine-cysteine with dioxygen.

@nl

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Inorganic Chemistry

P1476

Controlling the chiral inversi ...... steine-cysteine with dioxygen.

@en

P2093

Amanda M Glass

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

Jennifer S Laurence

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

Mary E Krause

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

Timothy A Jackson

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

P2860

Nickel Superoxide Dismutase Structure and Mechanism†

Spectroscopic and computational studies of Ni superoxide dismutase: electronic structure contributions to enzymatic function.

Sequence-specific Ni(II)-dependent peptide bond hydrolysis for protein engineering. Combinatorial library determination of optimal sequences.

Kinetics of racemization of amino acids as a function of pH.

Spectroscopic and computational investigation of three Cys-to-Ser mutants of nickel superoxide dismutase: insight into the roles played by the Cys2 and Cys6 active-site residues.

Dipeptide-based models of nickel superoxide dismutase: solvent effects highlight a critical role to Ni-S bonding and active site stabilization.

Metallopeptide based mimics with substituted histidines approximate a key hydrogen bonding network in the metalloenzyme nickel superoxide dismutase

Influence of the metal complex-to-peptide linker on the synthesis and properties of bioactive CpMn(CO)3 peptide conjugates.

Novel tripeptide model of nickel superoxide dismutase.

MAPping the chiral inversion and structural transformation of a metal-tripeptide complex having ni-superoxide dismutase activity.

P304

10055-10063

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scholarly article

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10.1021/IC301717Q

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18

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51

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2012-08-28T00:00:00Z

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22928993

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3939776

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