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A F420-dependent NADP reductase in the extremely thermophilic sulfate-reducing Archaeoglobus fulgidus

MPS-Authors

Kunow,  Jasper
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

Schwörer,  Beatrix
Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps- Universität, Marburg;
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thauer,  Rudolf K.       
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Kunow, J., Schwörer, B., Stetter, K. O., & Thauer, R. K. (1993). A F420-dependent NADP reductase in the extremely thermophilic sulfate-reducing Archaeoglobus fulgidus. Archives of Microbiology, 160(3), 199-205. doi:10.1007/BF00249125.


Cite as: https://hdl.handle.net/21.11116/0000-000F-91DD-4
Abstract
Archaeoglobus fulgidus, a sulfate-reducing Archaeon with a growth temperature optimum of 83°C, uses the 5-deazaflavin coenzyme F420 rather than pyridine nucleotides in catabolic redox processes. The organism does, however, require reduced pyridine nuclcotides for biosynthetic purposes. We describe here that the Archaeon contains a coenzyme F420-dependent NADP reductase which links anabolism to catabolism. The highly thermostable enzyme was purfied 3600-fold by affinity chromatography to apparent homogeneity in a 60% yield. The native enzyme with an apparent molecular mass of 55 kDa was composed of only one type of subunit of apparent molecular mass of 28 kDa. Spectroscopic analysis of the enzyme did not reveal the presence of any chromophoric prosthetic group. The purified enzyme catalyzed the reversible reduction of NADP (apparent KM 40 μM) with reduced F420 (apparent KM 20μM) with a specific activity of 660 U/mg (apparent Vmax) at pH 8.0 (pH optimum) and 80°C (temperature optimum). It was specific for both coenzyme F420 and NADP. Sterochemical investigations showed that the F420-dependent NADP reductase was Si face specific with respect to C5 of F420 and Si face specific with respect to C4 of NADP.