Characterization of the frhAGB-encoding hydrogenase from a non-methanogenic hyperthermophilic archaeon
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- 作者：Jeong Ho Jeon (1) (3)
Jae Kyu Lim (1)
Min-Sik Kim (1)
Tae-Jun Yang (1)
Seong-Hyuk Lee (1) (2)
Seung Seob Bae (1) (2)
Yun Jae Kim (1)
Sang Hee Lee (3)
Jung-Hyun Lee (1) (2)
Sung Gyun Kang (1) (2)
Hyun Sook Lee (1) (2) - 关键词：F420 ; reducing hydrogenase ; Thermococcus onnurineus NA1 ; FrhAGB
- 刊名：Extremophiles
- 出版年：2015
- 出版时间：January 2015
- 年：2015
- 卷：19
- 期：1
- 页码：109-118
- 全文大小：1,786 KB
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Jae Kyu Lim (1)
Min-Sik Kim (1)
Tae-Jun Yang (1)
Seong-Hyuk Lee (1) (2)
Seung Seob Bae (1) (2)
Yun Jae Kim (1)
Sang Hee Lee (3)
Jung-Hyun Lee (1) (2)
Sung Gyun Kang (1) (2)
Hyun Sook Lee (1) (2)
1. Marine Biotechnology Research Division, Korea Institute of Ocean Science and Technology, Ansan, South Korea
3. Department of Biological Sciences, National Leading Research Laboratory, Myongji University, Yongin, South Korea
2. Department of Marine Biotechnology, Korea University of Science and Technology, Daejeon, South Korea - ISSN：1433-4909
文摘
The F420-reducing hydrogenase has been known as a key enzyme in methanogenesis. Its homologs have been identified in non-methanogenic hyperthermophilic archaea, including Thermococcus onnurineus NA1, but neither physiological function nor biochemical properties have been reported to date. The enzyme of T. onnurineus NA1 was distinguished from those of other methanogens and the members of the family Desulfurobacteriaceae with respect to the phylogenetic distribution of the α and β subunits, organization of frhAGB genes and conservation of F420-coordinating residues. RT-qPCR and Western blot analyses revealed frhA gene is not silent but is expressed in T. onnurineus NA1 grown in the presence of sulfur, carbon monoxide, or formate. The trimeric enzyme complex was purified to homogeneity via affinity chromatography from T. onnurineus NA1 and exhibited catalytic activity toward the electron acceptors such as viologens and flavins but not the deazaflavin coenzyme F420. This is the first biochemical study on the function of the frhAGB-encoding enzyme from a non-methanogenic archaea.