title: Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: the molecular basis of cooperativity.
abstract: The NMR structure of the oxidised wild-type cytochrome c3 from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem-haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution.
authors.affiliation: Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780-156 Oeiras, Portugal.
authors.forename: Ana C
authors.initials: AC
authors.lastname: Messias
authors.forename: António P
authors.initials: AP
authors.lastname: Aguiar
authors.forename: Lorraine
authors.initials: L
authors.lastname: Brennan
authors.forename: Carlos A
authors.initials: CA
authors.lastname: Salgueiro
authors.forename: Lígia M
authors.initials: LM
authors.lastname: Saraiva
authors.forename: António V
authors.initials: AV
authors.lastname: Xavier
authors.forename: David L
authors.initials: DL
authors.lastname: Turner
mesh_terms: D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000737:chemistry* / Q000235:genetics*; D016969:Desulfovibrio vulgaris / Q000737:chemistry* / Q000235:genetics*; D005290:Ferric Compounds / Q000737:chemistry*; D006418:Heme / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010084:Oxidation-Reduction; D010100:Oxygen / Q000008:administration & dosage / Q000378:metabolism; D017354:Point Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions
chemical_list: D003574:Cytochrome c Group; D005290:Ferric Compounds; D012996:Solutions; D006418:Heme; C017165:cytochrome c(3); D010100:Oxygen