Structural basis for bacterial energy extraction from atmospheric hydrogen.
Structural basis for bacterial energy extraction from atmospheric hydrogen.
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DOI：
10.1038/s41586-023-05781-7
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发表时间：
2023-03
期刊：
影响因子：
64.8
通讯作者：
Greening, Chris
中科院分区：
文献类型：
--
作者：
Grinter, Rhys;Kropp, Ashleigh;Venugopal, Hari;Senger, Moritz;Badley, Jack;Cabotaje, Princess R.;Jia, Ruyu;Duan, Zehui;Huang, Ping;Stripp, Sven T.;Barlow, Christopher K.;Belousoff, Matthew;Shafaat, Hannah S.;Cook, Gregory M.;Schittenhelm, Ralf B.;Vincent, Kylie A.;Khalid, Syma;Berggren, Gustav;Greening, Chris
各种好氧细菌利用大气中的氢气作为生长和生存的能源。这一具有全球意义的过程调节了大气的组成，增强了土壤生物多样性，并推动了极端环境中的初级生产。大气中氢气的氧化被归因于[NiFe]氢酶超家族中的未知成员。然而，这些酶如何克服在催化毒物O2的环境水平中氧化皮摩尔水平的氢气这一非凡的催化挑战，以及衍生的电子如何转移到呼吸链，仍有待解决。在这里，我们测定了耻垢分枝杆菌氢酶Huc的冷冻电子显微镜结构，并对其作用机理进行了探讨。Huc是一种高效的氧不敏感酶，它将大气中氢气的氧化与呼吸电子载体孟喹酮的氢化偶联。HUC使用狭窄的疏水气体通道，以O2为代价选择性地结合大气中的H2，而3[3Fe-4S]团簇调节了酶的性质，因此大气中H2的氧化在能量上是可行的。HUC催化亚基在膜相关的茎周围形成一个八聚体833kDa复合体，该复合体运输和还原膜上的孟喹酮94 ä。这些发现为大气中重要的生物地球化学和生态氧化过程提供了机制基础，揭示了一种依赖于远程苯醌传输的能量耦合模式，并为开发氧化环境空气中氢气的催化剂铺平了道路。对耻垢分枝杆菌氢酶Huc的结构和生化研究提供了对[NiFe]氢酶如何氧化微量大气中的氢并转移通过醌运输释放的电子的见解。
Diverse aerobic bacteria use atmospheric H2 as an energy source for growth and survival. This globally significant process regulates the composition of the atmosphere, enhances soil biodiversity and drives primary production in extreme environments. Atmospheric H2 oxidation is attributed to uncharacterized members of the [NiFe] hydrogenase superfamily. However, it remains unresolved how these enzymes overcome the extraordinary catalytic challenge of oxidizing picomolar levels of H2 amid ambient levels of the catalytic poison O2 and how the derived electrons are transferred to the respiratory chain. Here we determined the cryo-electron microscopy structure of the Mycobacterium smegmatis hydrogenase Huc and investigated its mechanism. Huc is a highly efficient oxygen-insensitive enzyme that couples oxidation of atmospheric H2 to the hydrogenation of the respiratory electron carrier menaquinone. Huc uses narrow hydrophobic gas channels to selectively bind atmospheric H2 at the expense of O2, and 3 [3Fe–4S] clusters modulate the properties of the enzyme so that atmospheric H2 oxidation is energetically feasible. The Huc catalytic subunits form an octameric 833 kDa complex around a membrane-associated stalk, which transports and reduces menaquinone 94 Å from the membrane. These findings provide a mechanistic basis for the biogeochemically and ecologically important process of atmospheric H2 oxidation, uncover a mode of energy coupling dependent on long-range quinone transport, and pave the way for the development of catalysts that oxidize H2 in ambient air. Structural and biochemical studies of the Mycobacterium smegmatis hydrogenase Huc provides insights into how [NiFe] hydrogenases oxidize trace amounts of atmospheric hydrogen and transfer the electrons liberated via quinone transport.
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DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
影响因子：
3.7
作者：
Greening, Chris;Villas-Boas, Silas G.;Cook, Gregory M.
通讯作者：
Cook, Gregory M.
影响因子：
5.5
作者：
Hess, Berk
通讯作者：
Hess, Berk
影响因子：
15
作者：
Fourmond, Vincent;Infossi, Pascale;Leger, Christophe
通讯作者：
Leger, Christophe
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH