Involvement of electrostatic interactions in cytochrome c complex formations.
Structural studies on various electron transfer complexes involving the tetrahemic cytochrome c3 provided evidence that one of the hemes (heme 4) is the interacting site on the molecule. The reactivity of this particular heme is allocated to the positive charges found around the heme group which are strongly involved in the electrostatic interaction processes. Electrostatic and hydrophobic effects in complex formation are considered on the basis of two electron transfer complex examples: the soluble cytochrome c-cytochrome c peroxidase and the membrane bound photosynthetic reaction center.
Guerlesquin
F
F
Unité de Bioénergétique et Ingénierie des Protéines, Marseille, France.
Dolla
A
A
Bruschi
M
M
D000595:Amino Acid Sequence; D003574:Cytochrome c Group / Q000737:chemistry*; D003578:Cytochrome-c Peroxidase / Q000737:chemistry; D003901:Desulfovibrio / Q000201:enzymology; D004563:Electrochemistry; D005418:Flavodoxin / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry; D012416:Rubredoxins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D017973:Tungsten Compounds / Q000737:chemistry
D003574:Cytochrome c Group; D005418:Flavodoxin; D045322:Photosynthetic Reaction Center Complex Proteins; D012416:Rubredoxins; D017973:Tungsten Compounds; C017165:cytochrome c(3); D003578:Cytochrome-c Peroxidase