Mechanism of aromatic hydroxylation in a copper monooxygenase model system. 1,2-methyl migrations and the NIH shift in copper chemistry

Journal Article · Wed Mar 25 04:00:00 EST 1992 · Journal of the American Chemical Society

DOI:https://doi.org/10.1021/ja00033a024· OSTI ID:450839

Nasir, M S; Cohen, B I; Karlin, K D ^[1]

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1. Johns Hopkins Univ., Baltimore, MD (United States)

The mechanism of aromatic hydroxylation for 2-methyl substituted analogues of copper complexes studied previously, namely [Cu{sub 2}(Me{sub 2}XYL-CH{sub 3})]{sup 2+} (4) and [Cu{sub 2}(XYL-CH{sub 3})]{sup 2+} (5) are described in detail. Manometric O{sub 2} uptake experiments and labeling studies were used to unravel the reaction pathway. The NIH shift mechanism is said to be operative in a copper monooxygenase model system involving dicopper ion complex mediated O{sub 2} hydroxylation of an arene substrate. Manometric O{sub 2} uptake experiments and labeling studies were used to unravel the reaction pathway. 66 refs., 7 figs.

• Sponsoring Organization: USDOE
• OSTI ID: 450839
• Journal Information: Journal of the American Chemical Society, Journal Name: Journal of the American Chemical Society Journal Issue: 7 Vol. 114; ISSN JACSAT; ISSN 0002-7863
• Country of Publication: United States
• Language: English

Related Subjects

40 CHEMISTRY
55 BIOLOGY AND MEDICINE
BASIC STUDIES
AROMATICS
CATALYTIC EFFECTS
CHEMICAL REACTION YIELD
COPPER COMPLEXES
ENZYMES
HYDROXYLATION
OXYGENASES
REDUCTION