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首页> 外文期刊>Journal of sciences, Islamic Republic of Iran >ELUCIDATION OF pK_a VALUES FOR ACTIVE SITE OF HORSERADISH PEROXIDASE AND BINDING STUDY OF INTERACTION WITH N-PHENYL BENZHYDROXAMIC ACID USING A SPECIAL DIFFERENCE SPECTROPHOTOMETRIC TECHNIQUE
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ELUCIDATION OF pK_a VALUES FOR ACTIVE SITE OF HORSERADISH PEROXIDASE AND BINDING STUDY OF INTERACTION WITH N-PHENYL BENZHYDROXAMIC ACID USING A SPECIAL DIFFERENCE SPECTROPHOTOMETRIC TECHNIQUE

机译：辣根过氧化物酶活性位点pK_a值的测定及与N-苯基苯甲醛肟酸相互作用的特殊差光分光光度法研究

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摘要

The binding behavior of a competitive inhibitor, N-phenylbenzhydroxamic acid (BHA) against horseradish peroxidase (HRP) was studied in order to understand and predict the interaction mechanism of hydrogen donors with the enzyme. The dissociation constants of the complexes of HRP-BHA, HRP-donor and HRP-BHA- azide were estimated at specified conditions by difference spectroscopy. The binding site of BHA and that of hydrogen donor were also detected by spectroscopic titration of HRP in the presence of BHA and specific amino acid modifiers. A histidine binding site with pK_a= 6.40 was detected for the binding of BHA. On the other hand, activity-pH measurements showed that the maximum interaction of BHA with HRP occurs at a minimum point of activity at pH=6.40. The catalytic behavior of His 42 in the kinetic mechanism of enzyme action was also discussed.
机译：为了理解和预测氢供体与酶的相互作用机理，研究了竞争性抑制剂N-苯基苯氧肟酸（BHA）与辣根过氧化物酶（HRP）的结合行为。通过差异光谱法在指定条件下估算HRP-BHA，HRP供体和HRP-BHA-叠氮化物的复合物的解离常数。在存在BHA和特定氨基酸修饰剂的情况下，通过光谱滴定HRP还可检测BHA和氢供体的结合位点。检测到pK_a ＝ 6.40的组氨酸结合位点与BHA的结合。另一方面，活性-pH测量显示BHA与HRP的最大相互作用发生在pH = 6.40的最小活性点。还讨论了His 42在酶作用动力学机制中的催化行为。

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