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Journal Article

Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis

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Ermler,  Ulrich       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Fujishiro, T., Tamura, H., Schick, M., Kahnt, J., Xie, X., Ermler, U., et al. (2013). Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis. Angewandte Chemie, International Edition in English, 52(48), 12555-12558. doi:10.1002/anie.201306745.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0024-D492-8
Abstract
One reaction step of the biosynthesis of [Fe]-hydrogenase-cofactor is elucidated by S. Shima et al. in their Communication on page 12555 ff. A structural genomics approach, in combination with model reactions and thorough product analysis by X-ray crystallography of the protein–product complexes, revealed that HcgB is the enzyme that catalyzes guanylylpyridinol formation from a 2,4-dihydroxypyridine derivative and guanosine triphosphate.