Biomimetic Carbene-Catalyzed Oxidations of Aldehydes Using TEMPO
Biomimetic Carbene-Catalyzed Oxidations of Aldehydes Using TEMPO
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DOI：
10.1002/anie.200802735
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发表时间：
2008-01-01
影响因子：
16.6
通讯作者：
Studer, Armido
中科院分区：
文献类型：
--
作者：
Guin, Joyram;De Sarkar, Suman;Studer, Armido
丙酮酸铁氧还蛋白氧化还原酶（PFOR）属于2-酮酸氧化还原酶家族，催化丙酮酸氧化脱羧形成乙酰辅酶A和CO2。[1]这种CoA依赖性酶使用焦磷酸硫胺素（TPP）作为额外的辅因子。厌氧脱羧是一个可逆的过程，在一次转换过程中获得的两个电子通过[Fe 4S 4]团簇转移到铁氧化还原酶。[1]氧化脱羧的初始步骤类似于需氧TPP依赖性2-酮酸脱氢酶的那些。[2]丙酮酸盐与A反应，质子转移后形成B，B随后进行CO2消除生成C（方案1）。电子转移到[Fe 4S 4]簇导致自由基阳离子D。虽然密集的研究（X射线
Pyruvate ferredoxin oxidoreductase (PFOR), which catalyzes the oxidative decarboxylation of pyruvate to form acetyl-CoA and CO2, belongs to the family of 2-keto acid oxidoreductases.[1] This CoA-dependent enzyme uses thiamine pyrophosphate (TPP) as an additional cofactor. The anaerobic decarboxylation is a reversible process, and the two electrons obtained during one turnover are transferred to ferredoxine via [Fe4S4] clusters.[1]The initial steps of the oxidative decarboxylation resemble those of the aerobic TPP-dependent 2-oxoacid dehydrogenases.[2] Pyruvate reacts with A to form B after proton transfer, and B subsequently undergoes CO2 elimination to generate C (Scheme 1). Electron transfer to a [Fe4S4] cluster leads to radical cation D. Although intensive studies (X-ray