Effective Conversion of Metmyoglobin to Oxymyoglobin by Cysteine-Substituted Polyphenols
Effective Conversion of Metmyoglobin to Oxymyoglobin by Cysteine-Substituted Polyphenols
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DOI：
10.1021/acs.jafc.5b05511
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发表时间：
2016-02-03
影响因子：
6.1
通讯作者：
Masuda, Akiko
中科院分区：
文献类型：
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作者：
Honda, Sari;Miura, Yukari;Masuda, Akiko
在半胱氨酸存在下，多酚的过氧化物酶催化氧化的反应产物显示出将metmyogolobin（MetMb）还原为明亮颜色的oxymyogolobin（MbO（2））的有效活性。用高效液相色谱法（HPLC）对儿茶素、绿原酸、二氢咖啡酸、羟基酪醇、去甲二氢愈创木酸和迷迭香酸的反应产物进行纯化，得到相应的S-半胱氨酰化合物，其结构经核磁共振（NMR）和质谱（MS）测定。半胱氨酰多酚在最初的1 h内表现出浓度依赖性的还原活性。但在1h后，有些化合物使MbO（2）的生成量减少。使用具有不同数量的半胱氨酸取代的羟基酪醇检查多酚中半胱氨酸硫取代的数量对MetMb还原和MbO（2）维持的影响;这些羟基酪醇由羟基酪醇和N-乙酰半胱氨酸甲酯合成。用两个N-乙酰半胱氨酸酯取代的羟基酪醇衍生物表现出最有效的还原活性，而对MbO（2）没有任何影响。
Reaction products from the peroxidase-catalyzed oxidation of polyphenols in the presence of cysteine showed a potent activity for reducing metmyogolobin (MetMb) to bright-colored oxymyogolobin (MbO(2)). High-performance liquid chromatography (HPLC) purification of the reaction products from catechin, chlorogenic acid, dihydrocaffeic acid, hydroxytyrosol, nordihydroguaiaretic acid, and rosmarinic acid afforded corresponding S-cysteinyl compounds, the structures of which were determined by nuclear magnetic resonance (NMR) spectroscopy and mass spectrometry (MS). The isolated cysteinyl polyphenols showed a concentration-dependent reducing activity for MetMb to MbO(2) for the initial 1 h. However, after 1 h, some of them decreased the amount of MbO(2) produced. The effect of the number of cysteinyl sulfur substitutions in polyphenols on both MetMb reduction and MbO(2) maintenance was examined using hydroxytyrosols with different numbers of cysteine substitutions; these hydroxytyrosols were synthesized from hydroxytyrosol and an N-acetylcysteine methyl ester. The hydroxytyrosol derivative substituted with two N-acetylcysteine esters exhibited the most effective reducing activity without any effect on MbO(2).