The architecture of the binding site in redox protein complexes: implications for fast dissociation.
Interprotein electron transfer is characterized by protein interactions on the millisecond time scale. Such transient encounters are ensured by extremely high rates of complex dissociation. Computational analysis of the available crystal structures of redox protein complexes reveals features of the binding site that favor fast dissociation. In particular, the complex interface is shown to have low geometric complementarity and poor packing. These features are consistent with the necessity for fast dissociation since the absence of close packing facilitates solvation of the interface and disruption of the complex.
Crowley
Peter B
PB
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. Da República, Apartado 127, 2781 901 Oeiras, Portugal. crowley@itqb.unl.pt
Carrondo
Maria Arménia
MA
D000596:Amino Acids / Q000737:chemistry; D001665:Binding Sites; D004579:Electron Transport; D007700:Kinetics; D046911:Macromolecular Substances; D008958:Models, Molecular; D015394:Molecular Structure; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D055672:Static Electricity
D000596:Amino Acids; D046911:Macromolecular Substances; D011506:Proteins