CO Binding to the FeV Cofactor of CO-Reducing Vanadium Nitrogenase at Atomic Resolution.
CO Binding to the FeV Cofactor of CO-Reducing Vanadium Nitrogenase at Atomic Resolution.
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DOI：
10.1002/anie.202010790
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发表时间：
2020-12-21
期刊：
影响因子：
--
通讯作者：
Einsle O
中科院分区：
文献类型：
--
作者：
Rohde M;Grunau K;Einsle O
固氮酶还原氮气，氮气是地球大气中含量最丰富的元素，由于其稳定的三键，在其他方面不会发生化学转化。钒固氮酶的突出之处在于它还能处理一氧化碳，一氧化碳是除H+以外的所有底物还原的已知抑制剂。CO的还原导致碳氢化合物的形成，具有类似于工业Fischer-Tropsch过程的生物技术应用潜力。在这里，我们报告了迄今为止最高分辨率的钒固氮酶结构，在1 ä分辨率下，CO在催化周转后结合到活性中心辅助因子上。CO桥接铁离子Fe2和Fe6，取代硫化物S2B，结合方式与以前关于钼固氮酶CO络合物的报道一致。我们讨论了当CO被去除时继续周转的结构后果，其中包括可能被OH−取代的CO，Q176D和K361D的移动，硫化物的返回和两个额外的水分子的出现，这些水分子是不存在于CO结合态的。一氧化碳是固氮酶生物固氮的非竞争性抑制剂，但也是该酶依赖钒的变体的底物，导致涉及C−C键形成的碳氢化合物的形成。CO结合到活性中心辅因子上的酶的1 á分辨晶体结构揭示了配体的结合方式和μ2-桥联硫化物的可逆取代。
Nitrogenases reduce N2, the most abundant element in Earth's atmosphere that is otherwise resistant to chemical conversions due to its stable triple bond. Vanadium nitrogenase stands out in that it additionally processes carbon monoxide, a known inhibitor of the reduction of all substrates other than H+. The reduction of CO leads to the formation of hydrocarbon products, holding the potential for biotechnological applications in analogy to the industrial Fischer–Tropsch process. Here we report the most highly resolved structure of vanadium nitrogenase to date at 1.0 Å resolution, with CO bound to the active site cofactor after catalytic turnover. CO bridges iron ions Fe2 and Fe6, replacing sulfide S2B, in a binding mode that is in line with previous reports on the CO complex of molybdenum nitrogenase. We discuss the structural consequences of continued turnover when CO is removed, which involve the replacement of CO possibly by OH−, the movement of Q176D and K361D, the return of sulfide and the emergence of two additional water molecules that are absent in the CO‐bound state. Carbon monoxide is a non‐competitive inhibitor of biological nitrogen fixation by the enzyme nitrogenase, but also a substrate for the vanadium‐dependent variant of the enzyme, leading to a formation of hydrocarbon products that involve C−C bond formation. A 1.0 Å resolution crystal structure of the enzyme with CO bound to the active site cofactor reveals the binding mode of the ligand and the reversible replacement of a μ2‐bridging sulfide.
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影响因子：
7.7
作者：
Spatzal T;Perez KA;Howard JB;Rees DC
通讯作者：
Rees DC
影响因子：
56.9
作者：
GEORGIADIS, MM;KOMIYA, H;REES, DC
通讯作者：
REES, DC
通过空间分辨异常分散细化进行了调查的氮酶femoco。
影响因子：
16.6
作者：
Spatzal T;Schlesier J;Burger EM;Sippel D;Zhang L;Andrade SL;Rees DC;Einsle O
通讯作者：
Einsle O
影响因子：
56.9
作者：
Einsle, O;Tezcan, FA;Rees, DC
通讯作者：
Rees, DC
DOI：
10.1098/rsta.2004.1539
发表时间：
2005-04-15
影响因子：
5
作者：
Rees, DC;Tezcan, FA;Howard, JB
通讯作者：
Howard, JB