[Electron paramagnetic resonance study of photosensitized transport and localization of electrons in enzyme-substrate complexes. Lysozyme and its inhibitor].
Biofizika, 1975/9-1975/10;20(5):788-92.
Bulargina TV, Pulatova MK, Kravchenko NA, Kuropteva ZU
PMID: 173401
Abstract
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.
MeSH terms
Acetylglucosamine; Electron Spin Resonance Spectroscopy; Electron Transport; Glucosamine; Light; Muramidase
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