Si-face stereospecificity at C5 of coenzyme F420 for F420H2 oxidase from 
methanogenic Archaea as determined by mass spectrometry

Seedorf, H.; Kahnt, J.; Pierik, A. J.; Thauer, R. K.

doi:10.1111/j.1742-4658.2005.04931.x

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Si-face stereospecificity at C5 of coenzyme F₄₂₀ for F₄₂₀H₂ oxidase from methanogenic Archaea as determined by mass spectrometry

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Seedorf, H.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Kahnt, J.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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

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https://doi.org/10.1111/j.1742-4658.2005.04931.x
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Citation

Seedorf, H., Kahnt, J., Pierik, A. J., & Thauer, R. K. (2005). Si-face stereospecificity at C5 of coenzyme F₄₂₀ for F₄₂₀H₂ oxidase from methanogenic Archaea as determined by mass spectrometry. The FEBS Journal, 272(20), 5337-5342. doi:10.1111/j.1742-4658.2005.04931.x.

Cite as: https://hdl.handle.net/21.11116/0000-0007-C7F3-6

Abstract

Coenzyme F420 is a 5-deazaflavin. Upon reduction, 1,5 dihydro-coenzyme F420 is formed with a prochiral centre at C5. All the coenzyme F420-dependent enzymes investigated to date have been shown to be Si-face stereospecific with respect to C5 of the deazaflavin, despite most F420-dependent enzymes being unrelated phylogenetically. In this study, we report that the recently discovered F420H2 oxidase from methanogenic Archaea is also Si-face stereospecific. The enzyme was found to catalyse the oxidation of (5S)-[5-2H1]F420H2 with O2 to [5-1H]F420 rather than to [5-2H]F420 as determined by MALDI-TOF MS. (5S)-[5-2H1]F420H2 was generated by stereospecific enzymatic reduction of F420 with (14a-2H2)-[14a-2H2] methylenetetrahydromethanopterin.