title: Single-crystal electron paramagnetic resonance study of cytochrome c3 from Desulfovibrio desulfuricans Norway Strain. Assignment of the heme midpoint redox potentials.
abstract: A single crystal of cytochrome c3 from Desulfovibrio desulfuricans Norway is studied by electron paramagnetic resonance at low temperature. The orientation of the principal axis corresponding to the largest g value is determined for the 12 heme groups in the crystal unit cell. The comparison of these directions to the normals to the heme planes, determined from the crystallographic data at 2.5 A resolution, gives strong evidence for the following assignment of the midpoint redox potentials to the heme groups H1 to H4, defined in the three-dimensional structure: -150 mV is assigned to H3, -300 mV to H4, -330 mV to H1 and -355 mV to H2. This assignment is in agreement with a partial correspondence previously established from an independent study performed on cytochrome c3 in solution.
authors.affiliation: Laboratoire d'Electronique des Milieux Condensés, URA-CNRS 784, Université de Provence, Centre de St. Jérôme, Marseille, France.
authors.forename: B
authors.initials: B
authors.lastname: Guigliarelli
authors.forename: P
authors.initials: P
authors.lastname: Bertrand
authors.forename: C
authors.initials: C
authors.lastname: More
authors.forename: R
authors.initials: R
authors.lastname: Haser
authors.forename: J P
authors.initials: JP
authors.lastname: Gayda
mesh_terms: D003574:Cytochrome c Group / Q000302:isolation & purification / Q000378:metabolism*; D003901:Desulfovibrio / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D006418:Heme / Q000378:metabolism; D010084:Oxidation-Reduction; D011487:Protein Conformation
chemical_list: D003574:Cytochrome c Group; D006418:Heme; C017165:cytochrome c(3)