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- W3131697990 abstract "Electron transfer (ET) through and between proteins is a frequently occurring biological process in both prokaryotes and eukaryotes. Understanding the principle behind the ET will help to understand the important biological processes like respiration and photosynthesis. Several studies have been carried out on amicyanin and variants created by site-directed mutagenesis as a model system to study ET, which revealed several factors affecting this process. Very fine structural features like the position of hydrogen atoms, orientation of water molecules, distribution of valance electrons are essential for understanding the biological activities like ET in detail. An earlier joint x-ray and neutron study on amicyanin reveal location of hydrogen atoms of every residue and orientation of water molecules (with both hydrogens) at oxidized state. The current study applied the unique feature of x-ray crystallography, valance electron density (charge density) to visualize ET through amicyanin. As the current study involve ultra-high-resolution x-ray data, it details the features which can be observed only at this resolution such as location of hydrogen atoms and orientation of water molecules. Data sets were collected for oxidized amicyanin (0.65Å), reduced amicyanin at pH 4.4 (0.67Å) and reduced amicyanin at pH 7.7 (0.75Å). PHENIX, SHELX and MoPro programs were used for refinement and analysis. The analysis of oxidized amicyanin data showed the experimentally determined location of hydrogen atoms for various residues and water molecules. The study analyzed ET hot spots in amicyanin, particularly around the copper site and along the electron transfer path in terms of valence electron density. Residual and static deformation electron density maps were calculated along with Laplacian maps. It revealed deformation of bond density for various important residues. Details will be presented." @default.
- W3131697990 created "2021-03-01" @default.
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- W3131697990 date "2021-02-01" @default.
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- W3131697990 title "Ultra-High Resolution and Charge-Density Studies on the Type-I Copper Protein Amicyanin, from Paracoccus Denitrificans" @default.
- W3131697990 doi "https://doi.org/10.1016/j.bpj.2020.11.932" @default.
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