Redox sulfur chemistry of the copper chaperone Atox1 is regulated by the enzyme glutaredoxin 1, the reduction potential of the glutathione couple GSSG/2GSH and the availability of Cu(i)

Metallomics

Volumn 6, Issue 4, 2014, Pages 793-808

  Brose, Jens ^a   La Fontaine, Sharon ^b   Wedd, Anthony G ^a   Xiao, Zhiguang ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

^b DEAKIN UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; COPPER; EXPERIMENTS; METAL IONS; PHYSIOLOGY; PROTEINS; SULFUR;

CATALYTIC FUNCTIONS; COPPER HOMEOSTASIS; MOLECULAR PROPERTIES; NEGATIVE POTENTIAL; PROTEIN SUBSTRATE; REDOX REGULATION; REDUCTION POTENTIAL; SULFUR CHEMISTRY;

ENZYMES;

ATOX1 PROTEIN; CHAPERONE; CUPROUS ION; CYSTINE; DISULFIDE; DITHIOL DERIVATIVE; GLUTAREDOXIN; GLUTAREDOXIN 1; GLUTATHIONE; GLUTATHIONE DISULFIDE; MERCAPTOETHANOL; SULFUR; THIOL; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CATALYSIS; CHEMISTRY; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME BINDING; METAL BINDING; OXIDATION; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION STATE; PRIORITY JOURNAL;

COPPER; GLUTAREDOXINS; GLUTATHIONE; HUMANS; METALLOCHAPERONES; MODELS, MOLECULAR; OXIDATION-REDUCTION; SULFUR; THERMODYNAMICS;

EID: 84897381356     PISSN: 17565901     EISSN: 1756591X     Source Type: Journal    
DOI: 10.1039/c4mt00020j     Document Type: Article

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