The function of two radical-SAM enzymes, HcgA and HcgG, in the biosynthesis of 
the [Fe]-hydrogenase cofactor

Arriaza-Gallardo, F. J.; Schaupp, S.; Zheng, Y.-C.; Abdul-Halim, M. F.; Hui-Jie, P.; Kahnt, J.; Angelidou, G.; Paczia, N.; Hu, X.; Costa, K.; Shima, S.

doi:10.1002/anie.202213239

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The function of two radical-SAM enzymes, HcgA and HcgG, in the biosynthesis of the [Fe]-hydrogenase cofactor

MPG-Autoren

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Arriaza-Gallardo, F. J.
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Schaupp, S.
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons264361

Zheng, Y.-C.
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254414

Kahnt, J.
Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Angelidou, G.
Core Facility Metabolomics and small Molecules Mass Spectrometry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;
Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons261240

Paczia, N.
Core Facility Metabolomics and small Molecules Mass Spectrometry, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254714

Shima, S.
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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https://doi.org/10.1002/anie.202213239
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Zitation

Arriaza-Gallardo, F. J., Schaupp, S., Zheng, Y.-C., Abdul-Halim, M. F., Hui-Jie, P., Kahnt, J., et al. (2022). The function of two radical-SAM enzymes, HcgA and HcgG, in the biosynthesis of the [Fe]-hydrogenase cofactor. Angewandte Chemie, International Edition in English, 61(50): e202213239. doi:10.1002/anie.202213239.

Zitierlink: https://hdl.handle.net/21.11116/0000-000B-4F98-2

Zusammenfassung

In biosynthesis of the iron-guanylylpyridinol (FeGP) cofactor, 6-carboxymethyl-5-methyl-4-hydroxy-2-pyridinol (1) is 3-methylated to form 2, then 4-guanylylated to form 3, and converted to the full cofactor. HcgA-G proteins catalyze biosynthetic reactions. Here, we report the function of two radical S-adenosyl methionine enzymes, HcgA and HcgG, using in vitro complementation experiments and purified enzymes. In vitro biosynthesis using the cell extract from the Methanococcus maripaludis DeltahcgA strain was complemented with HcgA or precursors 1, 2 or 3. The results suggested that HcgA catalyzes the biosynthetic reaction that forms 1. We demonstrated the formation of 1 by HcgA using the 3-kDa cell extract filtrate as the substrate. Biosynthesis in the DeltahcgG system was recovered by HcgG but not by 3, which indicated that HcgG catalyzes the reactions after biosynthesis of 3. The data indicated that HcgG contributes to the formation of CO and completes biosynthesis of the FeGP cofactor.