Conversion of fatty aldehydes into alk (a/e)nes by in vitroreconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system

doi:10.1186/1754-6834-6-86

	Conversion of fatty aldehydes into alk (a/e)nes by in vitroreconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system
	Zhang,Jingjing 1,2; Lu,Xuefeng 1; Li,Jian-Jun 1
刊名	Biotechnology for Biofuels
	2013-06-08
卷号	6 期号:1
关键词	Biofuels Fatty alk(a/e)ne Synechococcus elongatus PCC7942 Aldehyde-deformylating oxygenase Ferredoxin Ferredoxin-NADP+ reductase The cognate reducing system
ISSN号	1754-6834
DOI	10.1186/1754-6834-6-86
英文摘要	AbstractBackgroundBiosynthesis of fatty alk(a/e)ne in cyanobacteria has been considered as a potential basis for the sunlight-driven and carbon-neutral bioprocess producing advanced solar biofuels. Aldehyde-deformylating oxygenase (ADO) is a key enzyme involved in that pathway. The heterologous or chemical reducing systems were generally used in in vitro ADO activity assay. The cognate electron transfer system from cyanobacteria to support ADO activity is still unknown.ResultsWe identified the potential endogenous reducing system including ferredoxin (Fd) and ferredoxin-NADP+ reductase (FNR) to support ADO activity in Synechococcus elongatus PCC7942. ADO (Synpcc7942_1593), FNR (SynPcc7942_0978), and Fd (SynPcc7942_1499) from PCC7942 were cloned, overexpressed, purified, and characterized. ADO activity was successfully supported with the endogenous electron transfer system, which worked more effectively than the heterologous and chemical ones. The results of the hybrid Fd/FNR reducing systems demonstrated that ADO was selective against Fd. And it was observed that the cognate reducing system produced less H2O2 than the heterologous one by 33% during ADO-catalyzed reactions. Importantly, kcat value of ADO 1593 using the homologous Fd/FNR electron transfer system is 3.7-fold higher than the chemical one.ConclusionsThe cognate electron transfer system from cyanobacteria to support ADO activity was identified and characterized. For the first time, ADO was functionally in vitro reconstituted with the endogenous reducing system from cyanobacteria, which supported greater activity than the surrogate and chemical ones, and produced less H2O2 than the heterologous one. The identified Fd/FNR electron transfer system will be potentially useful for improving ADO activity and further enhancing the biosynthetic efficiency of hydrocarbon biofuels in cyanobacteria.
语种	英语
出版者	BioMed Central
WOS记录号	BMC:10.1186/1754-6834-6-86
内容类型	期刊论文
源URL	[http://ir.qibebt.ac.cn/handle/337004/12599]
专题	中国科学院青岛生物能源与过程研究所
通讯作者	Lu,Xuefeng; Li,Jian-Jun
作者单位	1.Chinese Academy of Sciences; Key Laboratory of Biofuels, Shandong Provincial Key Laboratory of Energy Genetics, Qingdao Institute of Bioenergy and Bioprocess Technology 2.University of Chinese Academy of Sciences
推荐引用方式 GB/T 7714	Zhang,Jingjing,Lu,Xuefeng,Li,Jian-Jun. Conversion of fatty aldehydes into alk (a/e)nes by in vitroreconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system[J]. Biotechnology for Biofuels,2013,6(1).
APA	Zhang,Jingjing,Lu,Xuefeng,&Li,Jian-Jun.(2013).Conversion of fatty aldehydes into alk (a/e)nes by in vitroreconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system.Biotechnology for Biofuels,6(1).
MLA	Zhang,Jingjing,et al."Conversion of fatty aldehydes into alk (a/e)nes by in vitroreconstituted cyanobacterial aldehyde-deformylating oxygenase with the cognate electron transfer system".Biotechnology for Biofuels 6.1(2013).