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体外[FeFe]-氢化酶和鐡氧还蛋白:NADP+-氧化还原酶之间(FNR)酶类的光合电子分区
光合裂解水偶联氢化酶催化产氢已被认可是一种可再生能源。多数可接受的(观点)是:产生氢对氧的敏感性伴同在氢化酶和NADPH-依赖二氧化碳固定间的竞争性为其商业化的主要限制(因素)。这里,我们提供的证据是在厌氧条件下有助于产氢,因其在体外存在一种光合电子流向产生的NADPH-显著地丢失(现象)。为了阐明这一竞争基础,我们生物能化了一种鉄氧还蛋白-氢化酶融合体,并且表征了在存在Fd,鉄氧还蛋白:NADP+-氧化还原酶(FNR),和NADP+(条件下)产氢动力学。在由鉄氧还蛋白-氢化酶融合体替代氢化酶,转换电子递体从FNR向氢化酶偏移,结果导致光合产氢速率增加。这些结果提示改进生物产氢一个新的方向,并且该手段有利于进一步明晰光合电子转移调控分区机理。
本摘要译自张曙光/保罗·金课题组新近发表在PNAS上的论文英文摘要,不准确之处敬请同工指出。
该论文在研究海藻产氢方面有新意,自然对于开发应用可再生氢能源有重要意义,正如作者所说:“:“这一研究过程有很大可能实现产业化”,“你必须懂得这一过程所产生的实用价值,从而将氢燃料生产发展到商业规模,这只是时间和金钱的问题”,“费用问题解决了,我们将加快其实现的速度”,英文摘要附后。
Photosynthetic electron partitioning between [FeFe]-hydrogenase and ferredoxin:NADP+-oxidoreductase (FNR) enzymes in vitro
Photosynthetic water splitting, coupled to hydrogenase-catalyzed hydrogen production, is considered a promising clean, renewablesource of energy. It is widely accepted that the oxygen sensitivity of hydrogen production, combined with competition betweenhydrogenases and NADPH-dependent carbon dioxide fixation are the main limitations for its commercialization. Here we provideevidence that, under the anaerobic conditions that support hydrogen production, there is a significant loss of photosyntheticelectrons toward NADPH production in vitro. To elucidate the basis for competition, we bioengineered a ferredoxin-hydrogenasefusion and characterized hydrogen production kinetics in the presence of Fd, ferredoxin:NADP+-oxidoreductase (FNR), and NADP+. Replacing the hydrogenase with a ferredoxin-hydrogenase fusion switched the bias of electron transfer from FNR to hydrogenaseand resulted in an increased rate of hydrogen photoproduction. These results suggest a new direction for improvement of biohydrogenproduction and a means to further resolve the mechanisms that control partitioning of photosynthetic electron transport.
作 者:Yacoby, Iftach; Pochekailov, Sergii; Toporik, Hila; Ghirardi, Maria L.; King, Paul W.; Zhang, Shuguang
期刊名称: Proceedings of the National Academy of Sciences
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