Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Influence of pH on radical reactions between kynurenic acid and amino acids tryptophan and tyrosine. Part II. Amino acids within the protein globule of lysozyme. / Zhuravleva, Yuliya S.; Sherin, Peter S.
в: Free Radical Biology and Medicine, Том 174, 10.2021, стр. 211-224.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Influence of pH on radical reactions between kynurenic acid and amino acids tryptophan and tyrosine. Part II. Amino acids within the protein globule of lysozyme
AU - Zhuravleva, Yuliya S.
AU - Sherin, Peter S.
N1 - Funding Information: The financial support of this work was provided by Russian Science Foundation, project 18-73-10014. Publisher Copyright: © 2021 Elsevier Inc.
PY - 2021/10
Y1 - 2021/10
N2 - An acidosis, a decrease of pH within a living tissue, may alter yields of radical reactions if participating radicals undergo partial or complete protonation. One of photosensitizers found in the human eye lens, kynurenic acid (KNA−), possesses pKa 5.5 for its radical form that is close to physiological pH 6.89 for a healthy lens. In this work we studied the influence of pH on mechanisms and products of photoinduced radical reactions between KNA− and amino acids tryptophan (Trp) and tyrosine (Tyr) within a globule of model protein, Hen White Egg Lysozyme (HEWL). Our results show that the rate constant of back electron transfer from kynurenyl to HEWL• radicals with the restoration of initial reagents – the major decay pathway for these radicals – does not change in the pH 3–7. The quantum yield of HEWL degradation is also pH independent, however a shift of pH from 7 to 5 completely changes the outcome of photoinduced damage to HEWL from intermolecular cross-linking to oxygenation. HPLC-MS analysis has shown that four of six Trp and all Tyr residues of HEWL are modified in different extents at all pH, but the lowering of pH from 7 to 5 significantly changes the direction of main photodamage from Trp62 to Trp108 located at the entrance and bottom of enzymatic center, respectively. A decrease of intermolecular cross-links via Trp62 is followed by an increase in quantities of intramolecular cross-links Tyr20-Tyr23 and Tyr23-Tyr53. The obtained results point out the competence of cross-linking and oxygenation reactions for Trp and Tyr radicals within a protein globule and significant increase of oxygenation to the total damage of protein in the case of cross-linking deceleration by coulombic repulsion of positively charged protein globules.
AB - An acidosis, a decrease of pH within a living tissue, may alter yields of radical reactions if participating radicals undergo partial or complete protonation. One of photosensitizers found in the human eye lens, kynurenic acid (KNA−), possesses pKa 5.5 for its radical form that is close to physiological pH 6.89 for a healthy lens. In this work we studied the influence of pH on mechanisms and products of photoinduced radical reactions between KNA− and amino acids tryptophan (Trp) and tyrosine (Tyr) within a globule of model protein, Hen White Egg Lysozyme (HEWL). Our results show that the rate constant of back electron transfer from kynurenyl to HEWL• radicals with the restoration of initial reagents – the major decay pathway for these radicals – does not change in the pH 3–7. The quantum yield of HEWL degradation is also pH independent, however a shift of pH from 7 to 5 completely changes the outcome of photoinduced damage to HEWL from intermolecular cross-linking to oxygenation. HPLC-MS analysis has shown that four of six Trp and all Tyr residues of HEWL are modified in different extents at all pH, but the lowering of pH from 7 to 5 significantly changes the direction of main photodamage from Trp62 to Trp108 located at the entrance and bottom of enzymatic center, respectively. A decrease of intermolecular cross-links via Trp62 is followed by an increase in quantities of intramolecular cross-links Tyr20-Tyr23 and Tyr23-Tyr53. The obtained results point out the competence of cross-linking and oxygenation reactions for Trp and Tyr radicals within a protein globule and significant increase of oxygenation to the total damage of protein in the case of cross-linking deceleration by coulombic repulsion of positively charged protein globules.
KW - Back electron transfer
KW - Cross-linking
KW - Kynurenic acid
KW - Lysozyme
KW - Oxygenation
KW - Protonation
KW - Radicals
KW - UV-A light
KW - Tyrosine
KW - Oxidation-Reduction
KW - Kynurenic Acid
KW - Tryptophan
KW - Chickens/metabolism
KW - Amino Acids
KW - Muramidase/metabolism
KW - Animals
KW - Female
KW - Hydrogen-Ion Concentration
UR - http://www.scopus.com/inward/record.url?scp=85112830997&partnerID=8YFLogxK
U2 - 10.1016/j.freeradbiomed.2021.08.001
DO - 10.1016/j.freeradbiomed.2021.08.001
M3 - Article
C2 - 34363946
AN - SCOPUS:85112830997
VL - 174
SP - 211
EP - 224
JO - Free Radical Biology and Medicine
JF - Free Radical Biology and Medicine
SN - 0891-5849
ER -
ID: 33979601