Ru(II)-diimine functionalized metalloproteins: From electron transfer studies to light-driven biocatalysis.
Ru(II)-diimine functionalized metalloproteins: From electron transfer studies to light-driven biocatalysis.
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DOI：
10.1016/j.bbabio.2015.09.004
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发表时间：
2016-05
期刊：
影响因子：
--
通讯作者：
Cheruzel L
中科院分区：
文献类型：
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作者：
Lam Q;Kato M;Cheruzel L
Ru(II)-二亚胺络合物独特的光化学性质有助于在金属酶中开展一系列开创性的电子转移研究。因此，在实验上确定远程电子转移的速率常数是可能的。这些研究为研究血红素蛋白中的活性中间体和设计光活化生物催化剂奠定了基础。各种金属酶，如氢酶、一氧化碳脱氢酶、固氮酶、漆酶和细胞色素P450 BM3已被Ru(II)-双亚胺配合物功能化。在可见光激发下，这些光敏化金属蛋白能够保持光催化活性，还原质子、乙炔、氰化氢和一氧化碳等小分子，或激活分子氧生成羟基化产物。因此，Ru(II)-二亚胺光敏剂能够将多个电子传递到埋藏在金属酶中的活性部位，从而绕过了对天然氧化还原伙伴的需要。在这篇综述中，我们将重点介绍光驱动生物催化剂的主要成就，这些成就源于广泛的电子转移研究。
The unique photochemical properties of Ru(II)-diimine complexes have helped initiate a series of seminal electron transfer studies in metalloenzymes. It has thus been possible to experimentally determine rate constants for long-range electron transfers. These studies have laid the foundation for the investigation of reactive intermediates in heme proteins and for the design of light-activated biocatalysts. Various metalloenzymes, such as hydrogenase, carbon monoxide dehydrogenase, nitrogenase, laccase and cytochrome P450 BM3 have been functionalized with Ru(II)-diimine complexes. Upon visible light-excitation, these photosensitized metalloproteins are capable of sustaining photocatalytic activity to reduce small molecules such as protons, acetylene, hydrogen cyanide and carbon monoxide or activate molecular dioxygen to produce hydroxylated products. The Ru(II)-diimine photosensitizers are hence able to deliver multiple electrons to metalloenzymes buried active sites circumventing the need for the natural redox partners. In this review, we will highlight the key achievements of the light-driven biocatalysts, which stem from the extensive electron transfer investigations.