Theoretical study of oxyhemocyanin active site: a possible insight on the first step of phenol oxidation by tyrosinase

Eisenstein, Odile; Giessner-Prettre, Claude; Maddaluno, J.; Stussi, Dominique; Weber, Jacques

doi:10.1016/0003-9861(92)90569-I

Scientific article

English

Theoretical study of oxyhemocyanin active site: a possible insight on the first step of phenol oxidation by tyrosinase

Contributors

Eisenstein, Odile; Giessner-Prettre, Claude; Maddaluno, J.; Stussi, Dominique; Weber, Jacques

Published in

Archives of biochemistry and biophysics, vol. 296, no. 24, 247

Publication date

1992

Abstract

Extended Huckel theory calculations have been carried out on a model of the oxyhemocyanin active site that includes six imidazoles, the two copper cations, and a dioxygen molecule. The results obtained for the very likely μ-η2:η2 arrangement of the dioxygen molecule show that the most favorable orientation of O2 is such that the two long Cu---N coordination bonds are perpendicular to the plane formed by the two metal atoms and O2. This arrangement leads to pentacoordinated coppers with a distorted square pyramidal geometry. The molecular electrostatic potential maps of the complexes exhibit a potential well located close to the peroxo anion midbond. The dependence of the energy and of the molecular electrostatic maps on the precise orientation and location of the imidazole rings has been investigated. These results, which show the important role played by the third remote imidazole ligand, are discussed in relation with the first step of tyrosinase-mediated phenol oxidation.

UNIGE affiliation entities

Faculté des sciences / Section de chimie et biochimie / Département de chimie physique

UNIGE research groups

Groupe Weber

Citation (ISO format)

EISENSTEIN, Odile et al. Theoretical study of oxyhemocyanin active site: a possible insight on the first step of phenol oxidation by tyrosinase. In: Archives of biochemistry and biophysics, 1992, vol. 296, n° 24, p. 247. doi: 10.1016/0003-9861(92)90569-I

Identifiers

PID : unige:2931
DOI : 10.1016/0003-9861(92)90569-I

Journal ISSN

0003-9861

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Theoretical study of oxyhemocyanin active site: a possible insight on the first step of phenol oxidation by tyrosinase

Contributors

Published in

Publication date

Abstract

UNIGE affiliation entities

UNIGE research groups

Citation (ISO format)

Identifiers

Journal ISSN

Technical informations

Creation

First validation

Update

Status update

Last indexation