AI Article Synopsis
- The F420-reducing hydrogenase enzyme plays a crucial role in methanogenesis, but its function in non-methanogenic hyperthermophilic archaea like Thermococcus onnurineus NA1 was previously unknown.
- Researchers found that the frhA gene is actively expressed in T. onnurineus NA1 when grown with sulfur, carbon monoxide, or formate, contrary to previous assumptions about its activity.
- The enzyme complex was successfully purified and demonstrated catalytic activity with certain electron acceptors, but not with the coenzyme F420, marking a significant biochemical discovery for non-methanogenic archaea.
Article Abstract
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.
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