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

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.

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 Creators:
Fujishiro, Takashi1, Author
Tamura, Haruka1, Author
Schick, Michael1, Author
Kahnt, Jörg1, Author
Xie, Xiulan2, Author
Ermler, Ulrich3, Author                 
Shima, Seigo1, Author
Affiliations:
1Max‐Planck‐Institut für terrestrische Mikrobiologie, 35043 Marburg, Germany, ou_persistent22              
2Department of Chemistry, Philipps‐Universität Marburg, 35032 Marburg, Germany, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: biosynthesis; cofactors, hydrogenases; protein structures; transferases
 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.

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Language(s): eng - English
 Dates: 2013-09-232013-08-012013-11-182013-11-25
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201306745
 Degree: -

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Title: Angewandte Chemie, International Edition in English
  Abbreviation : Angew. Chem., Int. Ed. Engl.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 52 (48) Sequence Number: - Start / End Page: 12555 - 12558 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/0570-0833