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EPR spectroscopy: A powerful technique for the structural and functional investigation of metalloproteins

✍ Scribed by Claude More; Valérie Belle; Marcel Asso; André Fournel; Guy Roger; Bruno Guigliarelli; Patrick Bertrand

Publisher: John Wiley and Sons
Year: 1999
Tongue: English
Weight: 294 KB
Volume: 5
Category: Article
ISSN: 1075-4261
DOI: 10.1002/(sici)1520-6343(1999)5:5+<s3::aid-bspy2>3.0.co;2-p

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✦ Synopsis

Numerous metal centers in proteins can be prepared in a redox state in which their ground state is paramagnetic. Complementary data provided by EPR, Mo ¨ssbauer, electron nuclear double resonance, magnetic circular dichroism, and NMR spectroscopies have therefore played a major role in the elucidation of the structure and function of these centers. Among those techniques the most commonly used is certainly EPR spectroscopy. In this article various aspects of the current applications of EPR to the structural and functional study of metalloproteins are presented. They are illustrated by recent studies carried out in our laboratory in the field of metalloenzymes and electron transfer systems. The power of numerical simulation techniques is emphasized throughout this work.

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