Reactivity of the laccase trinuclear copper active site with dioxygen: An x-ray absorption edge study

Journal Article · Tue Mar 13 23:00:00 EST 1990 · Journal of the American Chemical Society; (USA)

DOI:https://doi.org/10.1021/ja00162a025· OSTI ID:6512108

Cole, J L; Tan, G O; Yang, E K; Hodgson, K O; Solomon, E I ^[1]

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1. Stanford Univ., CA (USA)

The multicopper oxidases (laccase, ascorbate oxidase, ceruloplasmin) catalyze the four-electron reduction of dioxygen to water. Laccase contains four Cu atoms: a type 1, a type 2, and a coupled binuclear type 3 center. Low-temperature MCD studies of laccase have demonstrated that the type 2 and type 3 centers comprise a trinuclear Cu cluster site and this model has been supported in a recent x-ray crystal structure of ascorbate oxidase. In the present study, x-ray absorption edge spectroscopy has been used to determine Cu oxidation states following reaction of reduced laccase derivatives with dioxygen, leading to a description of which of the Cu centers is required for reactivity.

• OSTI ID: 6512108
• Journal Information: Journal of the American Chemical Society; (USA), Journal Name: Journal of the American Chemical Society; (USA) Vol. 112:6; ISSN 0002-7863; ISSN JACSA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
COPPER
DATA
DATA ANALYSIS
ELEMENTS
ENZYMES
EXPERIMENTAL DATA
INFORMATION
MEASURING INSTRUMENTS
MEASURING METHODS
METALS
NUMERICAL DATA
REACTIVITY
TRANSITION ELEMENTS