Theory and practice of electron transfer within protein-protein complexes: application to the multidomain binding of cytochrome c by cytochrome c peroxidase

Article Abstract:

The kinetics of the electron transfer (ET) in protein-protein complexes depend on the extent and stoichiometry binding, and the interfacial dynamics of docking. The ET within protein-protein complexes produces noncovalent complexes. Cytochrome c peroxidase (CcP) forms a multidomain 2:1 binding complex of cytochrome c. The reduction of the Trp radical by electron transfer occurs under conditions of slow equilibration of CcP-II(sub h) and CcP-II(sub r). The reduction is a two-step process and occurs at the high affinity domain.

Observations, Cytochrome c, Peroxidase

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Electron-attachment reactions in molecular clusters

Article Abstract:

Electron-attachment reactions by isolated molecules and van der Waals clusters were observed for oxygen clusters, homogeneous clusters of polyatomic molecules and heterogeneous clusters. The reactions were studied by experiments using supersonic beams, seeded beam technique, trochoidal electron monochromator and time-of-flight technique. It was shown that interactions of low-energy electrons were possible with condensed matter.

Methods, Analysis, Condensed matter, Excited state chemistry, Scattering (Physics), Resonance, Resonance (Physics), Time-of-flight mass spectrometry, Complex compounds, Coordination compounds

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Interprotein electron transfer

Article Abstract:

Hemoglobin and cytochrome c protein compounds undergo protein-to-protein electron-transfer (ET) reactions. The reaction process exhibits dependence on protein distance, but the increasing effect of through-bonds on electronic coupling, limits the distance-dependence on intraprotein reactions. Furthermore, the binding properties of proteins determine the type of interacting physiological or nonphysiological ET partners.

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