Evidence for Electron Transfer from the Bidirectional Hydrogenase to the Photosynthetic Complex I (NDH-1) in the Cyanobacterium Synechocystis sp. PCC 6803.

Evidence for Electron Transfer from the Bidirectional Hydrogenase to the Photosynthetic Complex I (NDH-1) in the Cyanobacterium Synechocystis sp. PCC 6803.
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DOI:
10.3390/microorganisms10081617
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发表时间:
2022-08-10
期刊:
影响因子:
4.5
通讯作者:
--
中科院分区:
生物学3区
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--
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蓝藻双向[NiFe]-氢化酶是一种五聚体酶。除了小型和大型氢酶亚基(HoxYH)外,它还包含一个与NAD(P)+和铁氧还蛋白相互作用的心肌黄酶模块(HoxEFU)。HoxEFU与典型呼吸复合物I的最外层亚基(NuoEFG)具有很强的相似性。光合复合物I(NDH-1)缺少这三个亚基。这导致了HoxEFU可能与NDH-1相互作用的想法。HoxEFUYH利用PSI的激发电子进行光氢产生,它催化逆反应并将电子送入光合电子传递。我们分析了蓝细菌集胞藻6803的氢化酶活性、光氢释放和氢吸收、呼吸和光合电子传递ΔhoxEFUYH以及具有功能失调的NDH-1(Δ ndhD 1/Δ ndhD 2)的敲除菌株。在Δ ndhD 1/Δ ndhD 2中,由于吸氢量减少,光生氢时间延长。与野生型细胞相比,来自氢氧化的电子必须遵循不同的路线进入该突变体的光合电子传递。此外,在ΔhoxEFUYH中呼吸减少,氢化酶在膜上的Δ ndhD 1/Δ ndhD 2定位受损。这些数据表明,电子转移从氢化酶的NDH-1复合物是直接的,通过结合的氢化酶的复合物,或间接的,通过一个额外的介质。
The cyanobacterial bidirectional [NiFe]-hydrogenase is a pentameric enzyme. Apart from the small and large hydrogenase subunits (HoxYH) it contains a diaphorase module (HoxEFU) that interacts with NAD(P)+ and ferredoxin. HoxEFU shows strong similarity to the outermost subunits (NuoEFG) of canonical respiratory complexes I. Photosynthetic complex I (NDH-1) lacks these three subunits. This led to the idea that HoxEFU might interact with NDH-1 instead. HoxEFUYH utilizes excited electrons from PSI for photohydrogen production and it catalyzes the reverse reaction and feeds electrons into the photosynthetic electron transport. We analyzed hydrogenase activity, photohydrogen evolution and hydrogen uptake, the respiration and photosynthetic electron transport of ΔhoxEFUYH, and a knock-out strain with dysfunctional NDH-1 (ΔndhD1/ΔndhD2) of the cyanobacterium Synechocystis sp. PCC 6803. Photohydrogen production was prolonged in ΔndhD1/ΔndhD2 due to diminished hydrogen uptake. Electrons from hydrogen oxidation must follow a different route into the photosynthetic electron transport in this mutant compared to wild type cells. Furthermore, respiration was reduced in ΔhoxEFUYH and the ΔndhD1/ΔndhD2 localization of the hydrogenase to the membrane was impaired. These data indicate that electron transfer from the hydrogenase to the NDH-1 complex is either direct, by the binding of the hydrogenase to the complex, or indirect, via an additional mediator.
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