Protein-mediated electron transfer

TL;DR: This review gives an overview about the structural organisation of different evolutionary lines of all enzymes capable of efficient dismutation of hydrogen peroxide, as well as major potential applications in biotechnology and clinical medicine justify further investigations.

TL;DR: In this paper, the intramolecular electron transfer (ET) rates in ruthenium-modified derivatives of the beta barrel blue copper protein Pseudomonas aeruginosa azurin were investigated.

TL;DR: Chemical modification, cross-linking, and site-directed mutagenesis experiments have confirmed the importance of the negative and hydrophobic patches in binding interactions with cytochromef and Photosystem I, and validated the model of two functionally significant electron transfer paths in plastocyanin.

TL;DR: Analysis of the simplest electron transfer pathways between the redox partners points out the importance of other factors such as energetics in determining the electron transfer rates.

TL;DR: Powerful first-order analysis of intraprotein electron transfer is developed from electron-transfer measurements both in biological and in chemical systems, finding selection of distance, free energy and reorganization energy are sufficient to define rate and directional specificity of biological electron transfer.

TL;DR: The crystal structure of the fully oxidized form of ascorbate oxidase from Zucchini has been refined at 1.90 A (1 A = 0.1 nm) resolution, using an energy-restrained least-squares refinement procedure.

TL;DR: High-resolution three-dimensional structural analyses of yeast iso-1-cytochrome c have now been completed in both oxidation states using isomorphous crystalline material and similar structure determination methodologies, showing that oxidation state-dependent changes are expressed for the most part in terms of adjustments to heme structure, movement of internally bound water molecules and segmental thermal parameter changes along the polypeptide chain.

TL;DR: Both ethidium bromide (EB + ) and N,N'-dimethyl-2,7-diazapyrenium dichloride (DAP 2+ ) intercalate between base pairs in calf-thymus DNA as discussed by the authors.