Research Article
The architecture of the binding site in redox protein complexes: Implications for fast dissociation
Peter B. Crowley,
Maria Arménia Carrondo,
Corresponding Author
Peter B. Crowley
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. Da República, Apartado 127, 2781 901 Oeiras, Portugal
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. Da República, Apartado 127, 2781 901 Oeiras, Portugal===Search for more papers by this authorMaria Arménia Carrondo
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. Da República, Apartado 127, 2781 901 Oeiras, Portugal
Search for more papers by this authorPeter B. Crowley,
Maria Arménia Carrondo,
Corresponding Author
Peter B. Crowley
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. Da República, Apartado 127, 2781 901 Oeiras, Portugal
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. Da República, Apartado 127, 2781 901 Oeiras, Portugal===Search for more papers by this authorMaria Arménia Carrondo
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Av. Da República, Apartado 127, 2781 901 Oeiras, Portugal
Search for more papers by this authorAbstract
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. Proteins 2004;55:000–000. © 2004 Wiley-Liss, Inc.
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