SCOPUS 정보 검색 플랫폼

Journal of the American Chemical Society

Volumn 132, Issue 6, 2010, Pages 2005-2015

Reaction mechanisms of the multicopper oxidase CueO from Escherichia coli support its functional role as a cuprous oxidase

(4) Djoko, Karrera Y a,b Chong, Lee Xin a Wedd, Anthony G a Xiao, Zhiguang a

a UNIVERSITY OF MELBOURNE (Australia)

b UNIVERSITY OF QUEENSLAND (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AEROBIC CONDITION; AIR-STABLE; BICINCHONINATE; BINDING PROTEINS; CHROMOPHORIC SUBSTRATES; COPPER ATOMS; COPPER REDUCTION; COPPER TOLERANCE; DIOXYGEN REDUCTION; ELECTRON TRANSFER; FREE LIGANDS; MICHAELIS-MENTEN KINETIC; MODEL SUBSTRATES; MULTICOPPER OXIDASE; NEGATIVE SHIFT; NEW APPROACHES; OXIDASE ACTIVITY; OXIDASE ENZYMES; PH BUFFERS; PHENOL OXIDATION; REACTION MECHANISM; STEADY-STATE KINETICS; SUBSTRATE SPECIFICITY; TWO-COMPONENT;

ELECTRON TRANSITIONS; ENZYMES; ESCHERICHIA COLI; OXIDATION; PH EFFECTS; PHENOLS; SUBSTRATES; SULFUR COMPOUNDS;

COPPER;

ANION; BINDING PROTEIN; BUFFER; COPPER DERIVATIVE; CUPROUS OXIDE; METHIONINE; MULTICOPPER OXIDASE; OXIDOREDUCTASE; OXYGEN; PHENOL; SYRINGOL; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CHEMICAL BINDING; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SPECIFICITY; ESCHERICHIA COLI; KINETICS; MICHAELIS CONSTANT; NONHUMAN; OXIDATION; PRECIPITATION; REACTION ANALYSIS; STEADY STATE; STOICHIOMETRY;

BUFFERS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; METALS; MODELS, MOLECULAR; MONOPHENOL MONOOXYGENASE; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN STRUCTURE, TERTIARY; THERMODYNAMICS;

EID: 77249131784 PISSN: 00027863 EISSN: 15205126 Source Type: Journal
DOI: 10.1021/ja9091903 Document Type: Article

Times cited : (89)

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