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Book Chapter

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


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

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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.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-40F8-4
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].