Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: the molecular basis of cooperativity.
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.
Messias
Ana C
AC
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Rua da Quinta Grande 6, 2780-156 Oeiras, Portugal.
Aguiar
António P
AP
Brennan
Lorraine
L
Salgueiro
Carlos A
CA
Saraiva
Lígia M
LM
Xavier
António V
AV
Turner
David L
DL
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
D003574:Cytochrome c Group; D005290:Ferric Compounds; D012996:Solutions; D006418:Heme; C017165:cytochrome c(3); D010100:Oxygen