Role of oxygen in reactions of photoconversion of protein molecules irradiated in the region of 'La and 'Lb bands of tryptophanyl absorption spectrum

Spectral-luminescent properties of chlorin e 6 and malate dehydrogenase complexes

“…It is usually assumed that in binding the dyes of tetrapyrrole nature with the macromolecules of proteins [29,[35][36][37], including the molecules of enzymes [12,13], the main mechanism that causes the quenching of the luminescence of tryptophan amino acid residues is the inductive-resonant transfer of the energy of electronic excitation from the donor to the acceptor. Thus, according to [29], the effectiveness of the transfer (E) from tryptophanyl of the HSA to chlorin is close to unity (E > 0.99).…”

“…4a and b). For comparison we note that, according to the literature data [12,13,29,30,[35][36][37], the quenching of the fluorescence of other proteins (LDH, HSA, BSA) by tetrapyrrole photosensitizers, including chlorin e 6 and its derivatives, is entirely or partially attributable to the inductive-resonant energy transfer.…”