Si-face stereospecificity at C5 of coenzyme F420 for F420H2 oxidase from methanogenic Archaea as determined by mass spectrometry |
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Authors: | Seedorf Henning Kahnt Jörg Pierik Antonio J Thauer Rudolf K |
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Institution: | Max Planck Institute for Terrestrial Microbiology, Marburg, Germany. |
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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. |
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