Details

Autor(en) / Beteiligte

• McLendon, George
• Hake, Richard
• Zhang, Qipan
• Corin, Alan

Titel

Reorganization Energies for Protein-to-Protein Electron Transfer and Interfacial Dynamics: "Playing Fast and Loose"

Ist Teil von

• Molecular crystals and liquid crystals (1991), 1991-01, Vol.194 (1), p.225-232

Ort / Verlag

Taylor & Francis Group

Erscheinungsjahr

1991

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• Recent work on electron transfer in protein-protein complexes is summarized. Detailed measurements of binding equilibria and binding dynamics have been obtained for several systems: cytochrome c:cytochrome c peroxidase (CCP), cytochrome c:cytochrome b 5 , and hemoglobin:hemoglobin reductase. For the cytc:ccp system binding and subsequent electron transfer have ben probed using site-directed mutagenesis. These results suggest that binding and recognition involve several, overlapping binding sites. Furthermore, sites exist for binding cytc(II) vs. cytc(III). Thus, electron transfer must involve diffusion along the protein surface which connects the oxidized and reduced sites. Those single site mutants which bind less strongly have a lower diffusion barrier and thus can undergo more rapid electron transfer. This coupling of interfacial motion to reaction may offer a natural explanation for the large reorganization energies observed in biological systems.