title: EPR spectroscopy: a powerful technique for the structural and functional investigation of metalloproteins.
abstract: Numerous metal centers in proteins can be prepared in a redox state in which their ground state is paramagnetic. Complementary data provided by EPR, Mössbauer, 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.
authors.affiliation: Laboratoire de Bioénergétique et Ingénierie des Protéines, Institut de Biologie Structurale et de Microbiologie, CNRS, Marseille, France.
authors.forename: C
authors.initials: C
authors.lastname: More
authors.forename: V
authors.initials: V
authors.lastname: Belle
authors.forename: M
authors.initials: M
authors.lastname: Asso
authors.forename: A
authors.initials: A
authors.lastname: Fournel
authors.forename: G
authors.initials: G
authors.lastname: Roger
authors.forename: B
authors.initials: B
authors.lastname: Guigliarelli
authors.forename: P
authors.initials: P
authors.lastname: Bertrand
mesh_terms: D000363:Agaricales / Q000201:enzymology; D000449:Aldehyde Reductase / Q000737:chemistry; D000465:Algorithms; D001426:Bacterial Proteins / Q000737:chemistry; D003198:Computer Simulation; D003300:Copper / Q000737:chemistry; D000458:Cyanobacteria / Q000201:enzymology; D003574:Cytochrome c Group / Q000737:chemistry; D003901:Desulfovibrio / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D004926:Escherichia coli / Q000201:enzymology; D006418:Heme / Q000737:chemistry; D007501:Iron / Q000737:chemistry; D042845:Laccase; D008667:Metalloproteins / Q000737:chemistry*; D008956:Models, Chemical; D016297:Mutagenesis, Site-Directed; D050901:Nitrate Reductase; D009565:Nitrate Reductases / Q000737:chemistry; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry
chemical_list: D001426:Bacterial Proteins; D003574:Cytochrome c Group; D008667:Metalloproteins; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D006418:Heme; D003300:Copper; C017165:cytochrome c(3); D007501:Iron; D010088:Oxidoreductases; D000449:Aldehyde Reductase; D042845:Laccase; D009565:Nitrate Reductases; D050901:Nitrate Reductase