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Cyanobacterial hydrogenases: diversity, regulation and applications

机译:蓝细菌氢化酶:多样性,调控和应用

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Cyanobacteria may possess two distinct nickel-iron (NiFe)-hydrogenases: an uptake enzyme found in N-2-fixing strains, and a bidirectional one present in both non-N-2-fixing and N-2-fixing strains. The uptake hydrogenase (encoded by hupSL) catalyzes the consumption of the H-2 produced during N-2 fixation, while the bidirectional enzyme (hoxEFUYH) probably plays a role in fermentation and/or acts as an electron valve during photosynthesis. hupSL constitute a transcriptional unit, and are essentially transcribed under N-2-fixing conditions. The bidirectional hydrogenase consists of a hydrogenase and a diaphorase part, and the corresponding five hox genes are not always clustered or cotranscribed. The biosynthesis/maturation of NiFe-hydrogenases is highly complex, requiring several core proteins. In cyanobacteria, the genes that are thought to affect hydrogenases pleiotropically (hyp), as well as the genes presumably encoding the hydrogenase-specific endopeptidases (hupW and hoxW) have been identified and characterized. Furthermore, NtcA and LexA have been implicated in the transcriptional regulation of the uptake and the bidirectional enzyme respectively. Recently, the phylogenetic origin of cyanobacterial and algal hydrogenases was analyzed, and it was proposed that the current distribution in cyanobacteria reflects a differential loss of genes according to their ecological needs or constraints. In addition, the possibilities and challenges of cyanobacterial-based H-2 production are addressed.
机译:蓝细菌可能拥有两种截然不同的镍铁(NiFe)氢化酶:一种在N-2-固定菌株中发现的摄取酶,和一种在非N-2固定菌株和N-2-固定菌株中都存在的双向酶。摄取的氢化酶(由hupSL编码)催化N-2固定过程中产生的H-2的消耗,而双向酶(hoxEFUYH)可能在发酵中起作用和/或在光合作用中充当电子阀。 hupSL构成一个转录单位,并且基本上在N-2固定条件下转录。双向加氢酶由加氢酶和心肌黄递酶部分组成,相应的五个hox基因并不总是成簇或共转录的。 NiFe氢化酶的生物合成/成熟非常复杂,需要几种核心蛋白。在蓝细菌中,已经鉴定并鉴定了被认为会多效性影响氢化酶(hyp)的基因以及可能编码氢化酶特异性内肽酶的基因(hupW和hoxW)。此外,NtcA和LexA分别与摄取和双向酶的转录调控有关。最近,分析了蓝细菌和藻类加氢酶的系统发生起源,并提出了蓝细菌中的电流分布根据基因的生态需要或限制反映了基因的差异损失。此外,解决了基于蓝细菌的H-2生产的可能性和挑战。

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