Electron transfer in Ruthenium-modified proteins

Article Abstract:

Ruthenium-modified (Ru) proteins, such as cytochromes, myoglobin and copper complexes, provide kinetically-measured intramolecular electron-transfer (ET) reactions. The Ru-modified metalloproteins possess two covalently-bonded redox sites, which must either have long-lived excited states or bimolecularly-generated kinetic intermediates. The ET parameters, tunneling matrix element and reorganization energy, are involved in verifying the rate constant for ET nonadiabatic reactions. Furthermore, the ET parameters determine the electronic-coupling strength of the metalloprotein complex.

Cytochromes, Ruthenium

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Mechanisms whereby mononuclear copper proteins functionalize organic substrates

Article Abstract:

The mononuclear copper protein complexes use dioxygen to functionalize organic substrates via a reversible interconversion of protein-bound copper between its cuprous and cupric states. The reaction yields peroxide due to a two-electron reduction of O2 as either an intermediate or as a product. One-electron reduction of dioxygen by the Cu(I) active site followed by a second electron coming from a remote Cu(I) site reduces the number of ligands attached to the metal ion.

Observations, Copper

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Peptide-mediated intramolecular electron transfer: long-range distance dependence

Article Abstract:

The modification of thedriving force and reorganization energy and the changing of donor and acceptor (D-A) properties resulted in the determination of intramolecular electron-transfer (ET) rates at long distances. The ET rate measurement involved the use of oligoprolines, which provided rapid onset of D-A spatial rigidity. Moreover, the appropriate use of spectator ligands and transition metal ions led to variations in driving force and reorganization energy.

Methods, Peptides, Radiation chemistry, Amino acids, Photochemistry

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