Hsieh Chun H, Makris Thomas M
University of South Carolina, Department of Chemistry and Biochemistry, 631 Sumter Street, Columbia, SC 29208, USA.
University of South Carolina, Department of Chemistry and Biochemistry, 631 Sumter Street, Columbia, SC 29208, USA.
Biochem Biophys Res Commun. 2016 Aug 5;476(4):462-466. doi: 10.1016/j.bbrc.2016.05.145. Epub 2016 May 28.
The efficient hydrogen peroxide-dependent hydroxylation and epoxidation of hydrocarbons is catalysed by a P450 fatty acid decarboxylase (OleT) active-site variant. The introduction of an acidic functionality in the protein framework circumvents the necessity for a carboxylate that is typically provided by the substrate for efficient H2O2 heterolysis. Spectroscopic and turnover studies show that the mutation eliminates the binding and metabolism of prototypical fatty acid substrates, but permits the oxidation of a broad range of inert hydrocarbon substrates.
一种P450脂肪酸脱羧酶（OleT）活性位点变体可催化碳氢化合物高效的过氧化氢依赖性羟基化和环氧化反应。在蛋白质框架中引入酸性官能团，避免了通常由底物提供的用于高效过氧化氢异裂的羧酸盐的必要性。光谱和周转研究表明，该突变消除了典型脂肪酸底物的结合和代谢，但允许氧化多种惰性碳氢化合物底物。
