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通过多光子激发选择性氧化C(sp3) -H键的酶激发配位聚合物
作者:小柯机器人 发布时间:2023/1/26 12:47:57


大连理工大学段春迎团队报道了通过多光子激发选择性氧化C(sp3) -H键的酶激发配位聚合物。相关研究成果于2023年1月19日发表于国际顶尖学术期刊《美国化学会杂志》。

大自然的蓝图为扩大催化中丰富金属的使用提供了基本原则。然而,在一个人工系统中同时模拟铜酶的结构和功能以实现选择性C–H键氧化面临着显著的挑战。

该文中,研究人员报道了一种利用双核Cu2S2Cl2簇复制CuA酶的相同结构和催化作用组装人工单加氧酶的新方法。设计的单加氧酶Cu-Cl-bpyc促进了明确的氧化还原电位,该电位最初通过光诱导的电子转移激活O2,并通过配体到金属电荷转移(LMCT)过程从原位形成的铜(II)中心的连续激发生成活性氯自由基。氯自由基选择性地从C(sp3)–H键中提取氢原子以生成自由基中间体;同时,O2-物种与模拟物相互作用,形成混合价态物种,提供具有铜单加氧酶固有产物选择性的所需氧化产物,并直接回收催化剂。该酶促方案具有优异的可回收性、良好的官能团耐受性和广泛的底物范围,包括一些生物学和药理学相关的靶点。

机理研究表明,C–H键断裂是速率决定步骤,亚铜相互作用对稳定活性氧物种至关重要。明确的结构特征和精细改性的催化性能为开发具有均匀和精确活性位点和高催化性能的稳健人工酶开辟了一条新途径。

附:英文原文

Title: Enzyme-Inspired Coordination Polymers for Selective Oxidization of C(sp3)–H Bonds via Multiphoton Excitation

Author: Huilin Huang, Xu Jing, Jiangtao Deng, Changgong Meng, Chunying Duan

Issue&Volume: January 19, 2023

Abstract: Nature’s blueprint provides the fundamental principles for expanding the use of abundant metals in catalysis; however, mimicking both the structure and function of copper enzymes simultaneously in one artificial system for selective C–H bond oxidation faces marked challenges. Herein, we report a new approach to the assembly of artificial monooxygenases utilizing a binuclear Cu2S2Cl2 cluster to duplicate the identical structure and catalysis of the CuA enzyme. The designed monooxygenase Cu-Cl-bpyc facilitates well-defined redox potential that initially activated O2 via photoinduced electron transfer, and generated an active chlorine radical via a ligand-to-metal charge transfer (LMCT) process from the consecutive excitation of the in situ formed copper(II) center. The chlorine radical abstracts a hydrogen atom selectively from C(sp3)–H bonds to generate the radical intermediate; meanwhile, the O2– species interacted with the mimic to form mixed-valence species, giving the desired oxidization products with inherent product selectivity of copper monooxygenases and recovering the catalyst directly. This enzymatic protocol exhibits excellent recyclability, good functional group tolerance, and broad substrate scope, including some biological and pharmacologically relevant targets. Mechanistic studies indicate that the C–H bond cleavage was the rate-determining step and the cuprous interactions were essential to stabilize the active oxygen species. The well-defined structural characters and the fine-modified catalytic properties open a new avenue to develop robust artificial enzymes with uniform and precise active sites and high catalytic performances.

DOI: 10.1021/jacs.2c09348

Source: https://pubs.acs.org/doi/10.1021/jacs.2c09348

 

期刊信息

JACS:《美国化学会志》,创刊于1879年。隶属于美国化学会,最新IF:16.383
官方网址:https://pubs.acs.org/journal/jacsat
投稿链接:https://acsparagonplus.acs.org/psweb/loginForm?code=1000

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