[Environment of tryptophan residues in proteins--a factor for stability to oxidative nitrosylation. I. Analysis of primary structure].

Micellar catalysis under aerobic conditions effectively accelerates oxidative nitrosylation because of solubilization of NO and O2 by protein membranes and hydrophobic nuclei. Nitrosylating intermediates NOx (NO2, N2O3, N2O4) form mainly in the hydrophobic phase, and therefore their solubility in aqueous phase is low and hydrolysis is rapid, local concentration of NOx in the hydrophobic phase being essentially higher than in aqueous. Tryptophan is a hydrophobic residue and can nitrosylate with the formation of isomer N-nitrosotryptophans (NOW). Without denitrosylation mechanism, the accumulation of NOW in proteins of NO-synthesizing organisms would be constant, and long-living proteins would contain essential amounts of NOW, which is however not the case. Using Protein Data Bank (more than 78,000 sequences) we investigated the distribution of tryptophan residues environment (22 residues on each side of polypeptide chain) in proteins with known primary structure. Charged and polar residues (D, H, K, N, Q, R, S) are more incident in the immediate surrounding of tryptophan (-6, -5, -2, -1, 1, 2, 4) and hydrophobic residues (A, F, I, L, V, Y) are more rare than in remote positions. Hence, an essential part of tryptophan residues is situated in hydrophilic environment, which decreases the nitrosylation velocity because of lower NOx concentration in aqueous phase and allows the denitrosylation reactions course via nitrosonium ion transfer on nucleophils of functional groups of protein and low-molecular compounds in aqueous phase.