铜（I）配合物与 HO 引发的芬顿样化学与酶过氧化物酶 C-H 羟化的关系。
Fenton-like Chemistry by a Copper(I) Complex and HO Relevant to Enzyme Peroxygenase C-H Hydroxylation.
机构信息
Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218, United States.
Department of Chemistry, Stanford University, Stanford, California 94305, United States.
出版信息
J Am Chem Soc. 2023 May 31;145(21):11735-11744. doi: 10.1021/jacs.3c02273. Epub 2023 May 17.
Lytic polysaccharide monooxygenases have received significant attention as catalytic convertors of biomass to biofuel. Recent studies suggest that its peroxygenase activity (i.e., using HO as an oxidant) is more important than its monooxygenase functionality. Here, we describe new insights into peroxygenase activity, with a copper(I) complex reacting with HO leading to site-specific ligand-substrate C-H hydroxylation. [Cu(TMGtren)] () (TMGtren = 1,1,1-Tris{2-[-(1,1,3,3-tetramethylguanidino)]ethyl}amine) and a dry source of hydrogen peroxide, (-TolP═O·HO) react in the stoichiometry, [Cu(TMGtren)] + HO → [Cu(TMGtren-OH)] + HO, wherein a ligand -methyl group undergoes hydroxylation giving TMGtren-OH. Furthermore, Fenton-type chemistry (Cu + HO → Cu-OH + ·OH) is displayed, in which (i) a Cu(II)-OH complex could be detected during the reaction and it could be separately isolated and characterized crystallographically and (ii) hydroxyl radical (·OH) scavengers either quenched the ligand hydroxylation reaction and/or (iii) captured the ·OH produced.
溶细胞多糖单加氧酶作为将生物质转化为生物燃料的催化转化器受到了广泛关注。最近的研究表明，其过氧化物酶活性（即使用 HO 作为氧化剂）比单加氧酶功能更为重要。在这里，我们描述了过氧化物酶活性的新见解，铜（I）配合物与 HO 反应导致配位体-底物 C-H 羟化的特异性。[Cu(TMGtren)]（）（TMGtren = 1,1,1-三{2-[-(1,1,3,3-四甲基胍基)]乙基}胺）和过氧化氢的干源（-TolP═O·HO）以化学计量比反应，[Cu(TMGtren)] + HO → [Cu(TMGtren-OH)] + HO，其中一个配位体-甲基发生羟化生成 TMGtren-OH。此外，还显示出芬顿型化学（Cu + HO → Cu-OH + ·OH），其中（i）可以在反应过程中检测到 Cu(II)-OH 配合物，并且可以单独分离并通过晶体学进行表征；（ii）羟基自由基（·OH）清除剂要么猝灭配体的羟化反应，要么（iii）捕获产生的·OH。
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