Hyperthermophilic flavin reductase from Sulfolobus solfataricus P2: production and biochemical characterization

Gun, Gokhan and Imamoglu, Rahmi and Tatli, Ozge and Yürüm, Yuda and Tarik Baykal, Ahmet and Dinler-Doganay, Gizem (2019) Hyperthermophilic flavin reductase from Sulfolobus solfataricus P2: production and biochemical characterization. Biotechnology and Applied Biochemistry, 66 (6). pp. 915-923. ISSN 0885-4513 (Print) 1470-8744 (Online)

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Nicotinamide adenine dinucleotide phosphate (NAD(P)H)-flavin oxidoreductases (flavin reductases) catalyze the reduction of flavin by NAD(P)H and provide the reduced form of flavin mononucleotide (FMN) to flavin-dependent monooxygenases. Based on bioinformatics analysis, we identified a putative flavin reductase gene, sso2055, in the genome of hyperthermophilic archaeon Sulfolobus solfataricus P2, and further cloned this target sequence into an expression vector. The cloned flavin reductase (EC. was purified to homogeneity and characterized further. The purified enzyme exists as a monomer of 17.8 kDa, free of chromogenic cofactors. Homology modeling revealed this enzyme as a TIM barrel, which is also supported by circular dichroism measurements revealing a beta-sheet rich content. The optimal pH for SSO2055 activity was pH 6.5 in phosphate buffer and the highest activity observed was at 120 °C within the measurable temperature. We showed that this enzyme can use FMN and flavin adenine dinucleotide (FAD) as a substrate to generate their reduced forms. The purified enzyme is predicted to be a potential flavin reductase of flavin-dependent monooxygenases that could be involved in the biodesulfurization process of S. solfataricus P2.
Item Type: Article
Uncontrolled Keywords: archaea; biodesulfurization; flavin reductase activity; hyperthermophile; oxidoreductase
Divisions: Faculty of Engineering and Natural Sciences > Academic programs > Biological Sciences & Bio Eng.
Faculty of Engineering and Natural Sciences
Depositing User: Yuda Yürüm
Date Deposited: 27 Jul 2023 21:23
Last Modified: 27 Jul 2023 21:23
URI: https://research.sabanciuniv.edu/id/eprint/46341

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