脱羧
氧化脱羧
黄素组
化学
单加氧酶
氧化磷酸化
基质(水族馆)
催化作用
儿茶酚
生物化学
酶
立体化学
组合化学
生物
生态学
细胞色素P450
作者
Tiago A. S. Brandão,Lucas A. Vieira,Simara S. de Araújo,Ronaldo Alves Pinto Nagem
标识
DOI:10.1016/bs.mie.2023.03.017
摘要
Salicylate hydroxylase (NahG) is a FAD-dependent monooxygenase in which the reduced flavin activates O2 coupled to the oxidative decarboxylation of salicylate to catechol or uncoupled from substrate oxidation to afford H2O2. This chapter presents different methodologies in equilibrium studies, steady-state kinetics, and identification of reaction products, which were important to understand the SEAr mechanism of catalysis in NahG, the role of the different FAD parts for ligand binding, the extent of uncoupled reaction, and the catalysis of salicylate's oxidative decarboxylation. These features are likely familiar to many other FAD-dependent monooxygenases and offer a potential asset for developing new tools and strategies in catalysis.
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