[Electron paramagnetic resonance study of photosensitized transport and localization of electrons in enzyme-substrate complexes. Lysozyme and its inhibitor].
Photosensitized electron transfer are studied in three systems: lysozyme, its inhibitors (oligosaccharides) and their enzyme-inhibitor complexes. Electron donors were either tryptophane amino acid residues of lysozyme or tryptophane. It is shown that N-acetyl group of inhibitor molecules is a single electron--acceptor group in the inhibitor molecule as well as in the lysozyme-inhibitor complex. It is stated that the localization of unpaired electrons in the mixtures of lysozyme modification products and substrate--inhibitors depends on the state of enzyme molecule.
D000117:Acetylglucosamine; D004578:Electron Spin Resonance Spectroscopy; D004579:Electron Transport; D005944:Glucosamine / Q000031:analogs & derivatives*; D008027:Light; D009113:Muramidase / Q000037:antagonists & inhibitors
D009113:Muramidase; D005944:Glucosamine; D000117:Acetylglucosamine
Izuchenie fotosensibilizirovannogi perenosa i lokalizatsii élektronov v ferment-substratnykh kompleksakh pri pomoshchi élektronnogo paramagnitnogo rezonansa. Lizotsim i ego ingibitory