Flavin-Based Electron Bifurcation, Ferredoxin, Flavodoxin, and Anaerobic Respiration With Protons (Ech) or NAD(+) (Rnf) as Electron Acceptors: A Historical Review.

Flavin-Based Electron Bifurcation, Ferredoxin, Flavodoxin, and Anaerobic Respiration With Protons (Ech) or NAD(+) (Rnf) as Electron Acceptors: A Historical Review.
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DOI:
10.3389/fmicb.2018.00401
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发表时间:
2018
影响因子:
5.2
通讯作者:
Thauer RK
Thauer RK
中科院分区:
生物学2区
文献类型:
--
作者:
Buckel W;Thauer RK

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基于黄素的电子分叉是一种新发现的机制,通过这种机制,来自NAD(P)H、辅酶F420H2、H2或甲酸盐的氢化物电子对被黄素蛋白裂解成具有比电子对更负的还原电位和更正的还原电位的单电子。通过这种机制,微生物产生低势电子来还原铁氧还蛋白(Fd)和黄曲霉毒素(FLD)。第一个例子发生在2008年,当时发现克鲁维梭菌的丁酰辅酶A脱氢酶电子转移黄素蛋白复合体(BCD-ETFAB)将铁氧还蛋白(E0‘=−420 mV)与NADH(−320 mV)的电还原作用与NADH将巴豆酰辅酶A还原为丁酰辅酶A(−10 mV)的过程偶联。紧随其后的是在恒温酵母中发现了依赖FD和NAD的电子分叉的[FeFe]-氢酶(HydABC)(2009),在各种细菌和古菌中发现了依赖FD和NAD的转氢酶(NfnAB)(2010),在产甲烷的古菌中发现了依赖FD和H2的异二硫化物还原酶(MvhADG-HdrABC)(2011),在伍迪醋杆菌中发现了依赖FD和NAD的咖啡酰CoA还原酶(CarCDE)(2013),在乌氏梭菌中发现了依赖FD和NAD的甲酸脱氢酶(HylABC-FdhF2)(2013)自乙酸梭菌中依赖于FD和NADP的[FeFe]-氢酶(HYTA-E)(2013),热醋酸梭菌中依赖FD(?)和NADH的亚甲基四氢叶酸还原酶(MetFV-HdrABC-MvhD)(2014),伍迪氏梭菌中依赖FD和NAD的乳酸脱氢酶(LctBCD)(2015),甲烷弧菌中依赖FD和F420H2的异二硫化物还原酶(HdrA2B2C2)(2017),以及依赖FD和NADH的泛喹酚还原酶(FixABCX)(2017)。迄今已知的电子分叉黄素蛋白复合体分为四个独立进化的组,即含有结合Fad的EtfAB(Cared,LctCB,FixBA),含有FMN的NuoF同系物(HyDB,HYTB或HylB),具有结合Fad的NfnB,或含有Fad的HDRA。除了膜相关蛋白FixABCX外,所有这些黄素蛋白都是细胞质的。这些生物体--在其中发现了它们--严格意义上是厌氧微生物,但有氧菌A.vinelandii除外。电子分叉复合体参与了丁酸发酵、产甲烷、产乙酰基、厌氧乳酸氧化、异化硫酸盐还原、厌氧脱芳构化、固氮和固碳等多种过程。它们通过能量转换铁氧还蛋白:NAD+还原酶复合体RnF或能量转换铁氧还蛋白依赖氢酶复合体Ech来促进能量守恒。这篇综述描述了这种机制是如何被发现的。
Flavin-based electron bifurcation is a newly discovered mechanism, by which a hydride electron pair from NAD(P)H, coenzyme F420H2, H2, or formate is split by flavoproteins into one-electron with a more negative reduction potential and one with a more positive reduction potential than that of the electron pair. Via this mechanism microorganisms generate low- potential electrons for the reduction of ferredoxins (Fd) and flavodoxins (Fld). The first example was described in 2008 when it was found that the butyryl-CoA dehydrogenase-electron-transferring flavoprotein complex (Bcd-EtfAB) of Clostridium kluyveri couples the endergonic reduction of ferredoxin (E0′ = −420 mV) with NADH (−320 mV) to the exergonic reduction of crotonyl-CoA to butyryl-CoA (−10 mV) with NADH. The discovery was followed by the finding of an electron-bifurcating Fd- and NAD-dependent [FeFe]-hydrogenase (HydABC) in Thermotoga maritima (2009), Fd-dependent transhydrogenase (NfnAB) in various bacteria and archaea (2010), Fd- and H2-dependent heterodisulfide reductase (MvhADG-HdrABC) in methanogenic archaea (2011), Fd- and NADH-dependent caffeyl-CoA reductase (CarCDE) in Acetobacterium woodii (2013), Fd- and NAD-dependent formate dehydrogenase (HylABC-FdhF2) in Clostridium acidi-urici (2013), Fd- and NADP-dependent [FeFe]-hydrogenase (HytA-E) in Clostridium autoethanogrenum (2013), Fd(?)- and NADH-dependent methylene-tetrahydrofolate reductase (MetFV-HdrABC-MvhD) in Moorella thermoacetica (2014), Fd- and NAD-dependent lactate dehydrogenase (LctBCD) in A. woodii (2015), Fd- and F420H2-dependent heterodisulfide reductase (HdrA2B2C2) in Methanosarcina acetivorans (2017), and Fd- and NADH-dependent ubiquinol reductase (FixABCX) in Azotobacter vinelandii (2017). The electron-bifurcating flavoprotein complexes known to date fall into four groups that have evolved independently, namely those containing EtfAB (CarED, LctCB, FixBA) with bound FAD, a NuoF homolog (HydB, HytB, or HylB) harboring FMN, NfnB with bound FAD, or HdrA harboring FAD. All these flavoproteins are cytoplasmic except for the membrane-associated protein FixABCX. The organisms—in which they have been found—are strictly anaerobic microorganisms except for the aerobe A. vinelandii. The electron-bifurcating complexes are involved in a variety of processes such as butyric acid fermentation, methanogenesis, acetogenesis, anaerobic lactate oxidation, dissimilatory sulfate reduction, anaerobic- dearomatization, nitrogen fixation, and CO2 fixation. They contribute to energy conservation via the energy-converting ferredoxin: NAD+ reductase complex Rnf or the energy-converting ferredoxin-dependent hydrogenase complex Ech. This Review describes how this mechanism was discovered.
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