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  Structure and function of [Fe]-hydrogenase and biosynthesis of the FeGP cofactor

Shima, S., Fujishiro, T., & Ermler, U. (2015). Structure and function of [Fe]-hydrogenase and biosynthesis of the FeGP cofactor. In M. Rögner (Ed.), Biohydrogen (pp. 127-144). Berlin: Walter de Gruyter GmbH.

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 Creators:
Shima, Seigo1, 2, Author           
Fujishiro, Takashi1, Author
Ermler, Ulrich3, Author                 
Affiliations:
1Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch-Strasse 10, 35043 Marburg, Germany, ou_persistent22              
2PRESTO, Japan Science and Technology Agency (JST), 4-1-8 Honcho Kawaguchi, 332-0012 Saitama, Japan, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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 Abstract: The three known types of hydrogenases catalyze reversible activation of H2 and heterolytic
cleavage to a hydride and a proton . [NiFe]- and [FeFe]-hydrogenases further
cleave the hydride to two electrons and a proton. [Fe]-hydrogenase (Hmd), the enzyme covered in this chapter, instead transfers the hydride to a substrate, methenyltetrahydromethanopterin
(methenyl-H4MPT+ ) (Figure 6.1) [1, 2]. The free-energy change of this reaction is – 5.5 kJ/mol. The reverse reaction, formation of H2 and methenyl-
H4MPT+, is favorable under acidic conditions [3, 4].
[Fe]-hydrogenase is involved in the methanogenic pathway of many hydrogenotrophic
methanogenic archaea , including members of the Methanopyrales, Methanobacteriales,
and Methanococcales. Under nickel-limiting conditions , [Fe]-hydrogenase is
overproduced and functions as the major hydrogenase enzyme in the methanogenic
pathway, in which it provides four electrons [5]. [Fe]-hydrogenase contains a mononuclear
iron-guanylyl pyridinol (FeGP) cofactor. In the cofactor, the low-spin Fe(II) is
coordinated with two cis-CO and fixed to the organic part, guanylyl pyridinol, with
its acyl-carbon and pyridinol-nitrogen; the iron site is covalently bound to a cysteine
residue [1].

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Language(s): eng - English
 Dates: 2015
 Publication Status: Issued
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1515/9783110336733.127
 Degree: -

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Title: Biohydrogen
Source Genre: Book
 Creator(s):
Rögner, Matthias1, Editor
Affiliations:
1 Ruhr-Universität Bochum, Fakultät für Biologie & Biotechnologie, Universitätsstrasse 150, 44780 Bochum, Germany, ou_persistent22            
Publ. Info: Berlin : Walter de Gruyter GmbH
Pages: - Volume / Issue: - Sequence Number: - Start / End Page: 127 - 144 Identifier: ISBN: 978-3-11-033645-0
ISBN: 9783110336733
DOI: 10.1515/9783110336733