Methanogenesis involves direct hydride transfer from H2 to an organic substrate

Huang, Gangfeng; Wagner, T.; Ermler, Ulrich; Shima, Seigo

doi:10.1038/s41570-020-0167-2

Cited by 37 publications

(27 citation statements)

References 82 publications

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“…The most widely studied [Fe]-hydrogenase is Hmd from Methanothermobacter marburgensis. Hmd catalyzes the reversible, H 2 -driven reduction of methenyl-tetrahydromethanopterin (methenyl-H 4 MPT + ) with H 2 to methylene-H 4 MPT and H + , an intermediate step during the reduction of CO 2 to methane [26]. Hmd is a homodimer [27] and harbors a unique iron-guanylyl pyridinol (FeGP) cofactor at the active site that is typical for [Fe]-hydrogenases.…”

Section: [Fe]-hydrogenase Production Systemsmentioning

confidence: 99%

“…However, Hmd and its FeGP cofactor were inactivated upon exposure to UV-A (320-400 nm) or blue-light (400-500 nm), which is a unique feature among the three types of hydrogenases [34]. This sensitivity to light and their ability to transfer only hydride ions but not electrons are the main obstacles to the use of these enzymes in technological applications [26]. Recent studies showed that the reconstitution of active [Fe]-hydrogenase in vitro is feasible ( Figure 1).…”

Section: [Fe]-hydrogenase Production Systemsmentioning

confidence: 99%

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Heterologous Hydrogenase Overproduction Systems for Biotechnology—An Overview

Fan

Neubauer

Lenz

et al. 2020

IJMS

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Hydrogenases are complex metalloenzymes, showing tremendous potential as H2-converting redox catalysts for application in light-driven H2 production, enzymatic fuel cells and H2-driven cofactor regeneration. They catalyze the reversible oxidation of hydrogen into protons and electrons. The apo-enzymes are not active unless they are modified by a complicated post-translational maturation process that is responsible for the assembly and incorporation of the complex metal center. The catalytic center is usually easily inactivated by oxidation, and the separation and purification of the active protein is challenging. The understanding of the catalytic mechanisms progresses slowly, since the purification of the enzymes from their native hosts is often difficult, and in some case impossible. Over the past decades, only a limited number of studies report the homologous or heterologous production of high yields of hydrogenase. In this review, we emphasize recent discoveries that have greatly improved our understanding of microbial hydrogenases. We compare various heterologous hydrogenase production systems as well as in vitro hydrogenase maturation systems and discuss their perspectives for enhanced biohydrogen production. Additionally, activities of hydrogenases isolated from either recombinant organisms or in vivo/in vitro maturation approaches were systematically compared, and future perspectives for this research area are discussed.

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Section: [Fe]-hydrogenase Production Systemsmentioning

confidence: 99%

Section: [Fe]-hydrogenase Production Systemsmentioning

confidence: 99%

Heterologous Hydrogenase Overproduction Systems for Biotechnology—An Overview

Fan

Neubauer

Lenz

et al. 2020

IJMS

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“…15 The monometallic [Fe]-hydrogenases do not catalyse hydrogen turnover per se but facilitate hydride transfer from a guanylylpridinol-coordinated iron site (Fe-GP) to an tetrahydromethanopterin cofactor (H4MPT). 16 Moreover, [Fe]-hydrogenases do not bind iron-sulphur clusters. While the molecular details of proton transfer in [NiFe]-and [FeFe]-hydrogenases are fairly well understood 17 , no such data exist for [Fe]-hydrogenase.…”

Section: Hydrogenasesmentioning

confidence: 99%

Operando Infrared Spectroscopy for the Analysis of Gas-processing Metalloenzymes

Stripp¹

2020

Preprint

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Earth-abundant transition metals like iron, nickel, copper, molybdenum, and vanadium have been identified as essential constituents of the cellular gas metabolism in all kingdoms of life. Associated with biological macromolecules, gas-processing metalloenzymes (GPMs) are formed that catalyse a variety of redox reactions. This includes the reduction of O2 to water by cytochrome c oxidase (‘complex IV’), the reduction of N2 to NH4 by nitrogenase, as well as the reduction of protons to H2 (and oxidation of the later) by hydrogenase. GPMs perform at ambient temperature and pressure, in the presence of water, and often extremely low educt concentrations, thus serving as natural examples for efficient catalysis. Facilitating the design of biomimetic catalysts, biophysicist thrive to understand the reaction principles of GPMs making use of various techniques. In this perspective, I will introduce Fourier-transform infrared spectroscopy in attenuated total reflection configuration (ATR FTIR) for the analysis of GPMs like cytochrome c oxidase, nitrogenase, and hydrogenase. Infrared spectroscopy provides information about the geometry and redox state of the catalytic cofactors, the protonation state of amino acid residues, the hydrogen-bonding network, and protein structural changes. I developed an approach to probe and trigger the reaction of GPMs by gas exchange experiments, exploring the reactivity of these enzymes with their natural reactants. This allows recording sensitive ATR FTIR difference spectra with seconds time resolution. Finally yet importantly, infrared spectroscopy is an electronically non-invasive technique that allows investigating protein samples under biologically relevant conditions, i.e., at ambient temperature and pressure, and in the presence of water.

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“…[Fe]-hydrogenase (Hmd) catalyzes the reversible hydride transfer to methenyltetrahydromethanopterin (methenyl-H 4 MPT + ) from H 2 ( Figure 1a) [1,2]. This reaction is involved in the hydrogenotrophic methanogenic pathway [2,3].…”

Section: Introductionmentioning

confidence: 99%

“…Many mimic complexes of the FeGP cofactor have been synthesized [2,[21][22][23][24][25][26]. Some of the mimics are composed of similar complex structures to the FeGP cofactor containing Fe(II) [27] or Mn(I) [25] as the metal center with two CO and pyridinol but lack the GMP moiety.…”

Section: Introductionmentioning

confidence: 99%

Crystal Structures of [Fe]-Hydrogenase from Methanolacinia paynteri Suggest a Path of the FeGP-Cofactor Incorporation Process

et al. 2020

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[Fe]-hydrogenase (Hmd) catalyzes the reversible heterolytic cleavage of H2, and hydride transfer to methenyl-tetrahydromethanopterin (methenyl-H4MPT+). The iron-guanylylpyridinol (FeGP) cofactor, the prosthetic group of Hmd, can be extracted from the holoenzyme and inserted back into the protein. Here, we report the crystal structure of an asymmetric homodimer of Hmd from Methanolacinia paynteri (pHmd), which was composed of one monomer in the open conformation with the FeGP cofactor (holo-form) and a second monomer in the closed conformation without the cofactor (apo-form). In addition, we report the symmetric pHmd-homodimer structure in complex with guanosine monophosphate (GMP) or guanylylpyridinol (GP), in which each ligand was bound to the protein, where the GMP moiety of the FeGP-cofactor is bound in the holo-form. Binding of GMP and GP modified the local protein structure but did not induce the open conformation. The amino-group of the Lys150 appears to interact with the 2-hydroxy group of pyridinol ring in the pHmd–GP complex, which is not the case in the structure of the pHmd–FeGP complex. Lys150Ala mutation decreased the reconstitution rate of the active enzyme with the FeGP cofactor at the physiological pH. These results suggest that Lys150 might be involved in the FeGP-cofactor incorporation into the Hmd protein in vivo.

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Methanogenesis involves direct hydride transfer from H2 to an organic substrate

Cited by 37 publications

References 82 publications

Heterologous Hydrogenase Overproduction Systems for Biotechnology—An Overview

Heterologous Hydrogenase Overproduction Systems for Biotechnology—An Overview

Operando Infrared Spectroscopy for the Analysis of Gas-processing Metalloenzymes

Crystal Structures of [Fe]-Hydrogenase from Methanolacinia paynteri Suggest a Path of the FeGP-Cofactor Incorporation Process

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