Intermolecular Electron Transfer Reactivity and Dynamics of Cytochrome c â•fi Nanoparticle Adducts

Intermolecular electron-transfer catalyzed on nanoparticle surfaces.

Surface-functionalized nanoparticles enhance the rate of electron transfer (ET) between Cyt c(Fe(2+)) and Co(phen)(3)(3+) by a factor of 10(5) through simultaneous electrostatic binding of an ET donor and acceptor.

Control of cytochrome c redox reactivity through off-pathway modifications in the protein hydrogen-bonding network.

Measurements of photoinduced Fe(2+)-to-Ru(3+) electron transfer (ET), supported by theoretical analysis, demonstrate that mutations off the dominant ET pathways can strongly influence the redox reactivity of cytochrome c. The effects arise from the change in the protein dynamics mediated by the intraprotein hydrogen-bonding network.

An hypothetical structure for an intermolecular electron transfer complex of cytochromes c and b5.

Effects of interface mutations on association modes and electron-transfer rates between proteins.

Although bonding networks determine electron-transfer (ET) rates within proteins, the mechanism by which structure and dynamics influence ET across protein interfaces is not well understood. Measurements of photochemically induced ET and subsequent charge recombination between Zn-porphyrin-substituted cytochrome c peroxidase and cytochrome c in single crystals correlate reactivity with defined ...

Complex formation and intermolecular electron transfer between flavocytochrome b2 in the crystal and cytochrome c.

The present study addresses the question whether tetrameric flavocytochrome b2 in the crystal is catalytically competent and, if so, whether it is possible to prepare a functional complex of the crystalline enzyme with its physiological electron acceptor cytochrome c. By single crystal microspectrophotometry we show that the native reduced enzyme can be oxidized by oxygen or ferricyanide and th...