Systematic perturbation of the trinuclear copper cluster in the multicopper oxidases: The role of active site asymmetry in its reduction of O2 to H2O

Journal of the American Chemical Society

Volumn 132, Issue 17, 2010, Pages 6057-6067

  Augustine, Anthony J ^a   Kjaergaard, Christian ^a   Qayyum, Munzarin ^a   Ziegler, Lynn ^c   Kosman, Daniel J ^c   Hodgson, Keith O ^a,b   Hedman, Britt ^b   Solomon, Edward I ^a,b  

^a STANFORD UNIVERSITY   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^c UNIVERSITY AT BUFFALO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; COPPER CLUSTER; CU ATOMS; DIOXYGENS; FOUR-ELECTRON REDUCTION; MULTICOPPER OXIDASE; ONE-ELECTRON OXIDATION; OXIDIZED STATE; PEROXIDE INTERMEDIATE; REDOX ACTIVITY; REDUCED-STATE; SPECTROSCOPIC FEATURES; STRUCTURAL ORIGIN; SYSTEMATIC PERTURBATIONS; TRINUCLEAR CLUSTER;

LIGANDS; OXIDATION; REDOX REACTIONS; SUBSTRATES;

COPPER;

COPPER DERIVATIVE; COPPER OXIDASE; OXYGEN; PEROXIDE; UNCLASSIFIED DRUG; WATER;

ARTICLE; ASYMMETRIC SYNTHESIS; ATOM; CHEMICAL REACTION; CHEMICAL STRUCTURE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; LIGAND BINDING; OXIDATION REDUCTION REACTION;

CATALYTIC DOMAIN; CERULOPLASMIN; COPPER; OXIDATION-REDUCTION; OXYGEN; SACCHAROMYCES CEREVISIAE PROTEINS; WATER;

EID: 77951694386     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja909143d     Document Type: Article

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