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Why Does the Active Form of Galactose Oxidase Possess a Diamagnetic Ground State?

✍ Scribed by Jochen Müller; Thomas Weyhermüller; Eckhard Bill; Peter Hildebrandt; Linda Ould-Moussa; Thorsten Glaser; Karl Wieghardt

Publisher
John Wiley and Sons
Year
1998
Tongue
English
Weight
160 KB
Volume
37
Category
Article
ISSN
0044-8249

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✦ Synopsis

The relative orientation of the two magnetic orbitals, the Cu d x 2-y 2 orbital and the half-occupied π orbital of the tyrosyl radical, is the key to answering the question in the title. The arrangement shown (Cu -O-C bond angle of about 130° and a dihedral angle of about 90° between the x,y plane of the Cu polyhedron and the tyrosyl ring plane) leads to an overlap of the orbitals, which results in a singlet ground state.

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✍ Fabrice Thomas; Gisèle Gellon; Isabelle Gautier-Luneau; Eric Saint-Aman; Jean-Lo 📂 Article 📅 2002 🏛 John Wiley and Sons 🌐 English ⚖ 100 KB 👁 2 views

Galactose oxidase (GOase) is a type II copper protein (68 kDa) that catalyzes the oxidation of primary alcohols to aldehydes with the concomitant reduction of molecular oxygen. [1] Its crystal structure [2] reveals a unique mononuclear copper site with two nitrogen (from histidine imidazole groups)