title: 1H-NMR study of the structural influence of Y64 substitution in Desulfovibrio vulgaris Hildenborough cytochrome c553.
abstract: Y64 has been replaced in cytochrome c553 from Desulfovibrio vulgaris Hildenborough by phenylalanine, leucine, valine, serine and alanine residues. An NMR study of structural variation induced in both oxidoreduction states of the molecule has been carried out by analysing observed chemical-shift variations. Dynamic changes were evidenced using NH exchange. We have observed that the substitution has a drastic effect on the stability of the molecule in the reduced state, although there is no effect on the reduction potential of the cytochrome. Y64-->F substitution induces particular effects on the NH exchange at the N-terminal, C-terminal and central alpha-helices and increases the stability of the oxidized molecule.
authors.affiliation: Unité de Bioénergétique et Ingénierie des Protéines, IBSM-CNRS, Marseille, France.
authors.forename: C
authors.initials: C
authors.lastname: Sebban-Kreuzer
authors.forename: L
authors.initials: L
authors.lastname: Blanchard
authors.forename: B
authors.initials: B
authors.lastname: Bersch
authors.forename: M J
authors.initials: MJ
authors.lastname: Blackledge
authors.forename: D
authors.initials: D
authors.lastname: Marion
authors.forename: A
authors.initials: A
authors.lastname: Dolla
authors.forename: F
authors.initials: F
authors.lastname: Guerlesquin
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D017124:Conserved Sequence; D003574:Cytochrome c Group / Q000737:chemistry*; D016969:Desulfovibrio vulgaris / Q000378:metabolism*; D006859:Hydrogen; D016297:Mutagenesis, Site-Directed; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D003574:Cytochrome c Group; D011994:Recombinant Proteins; C083951:cytochrome c553; D006859:Hydrogen