Complex multimeric [FeFe] hydrogenases : biochemistry, physiology and new opportunities for the hydrogen economy
- Hydrogenases are key enzymes of the energy metabolism of many microorganisms. Especially in anoxic habitats where molecular hydrogen (H2) is an important intermediate, these enzymes are used to expel excess reducing power by reducing protons or they are used for the oxidation of H2 as energy and electron source. Despite the fact that hydrogenases catalyze the simplest chemical reaction of reducing two protons with two electrons it turned out that they are often parts of multimeric enzyme complexes catalyzing complex chemical reactions with a multitude of functions in the metabolism. Recent findings revealed multimeric hydrogenases with so far unknown functions particularly in bacteria from the class Clostridia. The discovery of [FeFe] hydrogenases coupled to electron bifurcating subunits solved the enigma of how the otherwise highly endergonic reduction of the electron carrier ferredoxin can be carried out and how H2 production from NADH is possible. Complexes of [FeFe] hydrogenases with formate dehydrogenases revealed a novel enzymatic coupling of the two electron carriers H2 and formate. These novel hydrogenase enzyme complex could also contribute to biotechnological H2 production and H2 storage, both processes essential for an envisaged economy based on H2 as energy carrier.
Author: | Kai SchuchmannGND, Nilanjan Pal ChowdhuryORCiDGND, Volker MüllerORCiD |
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URN: | urn:nbn:de:hebis:30:3-492819 |
DOI: | https://doi.org/10.3389/fmicb.2018.02911 |
ISSN: | 1664-302X |
Pubmed Id: | https://pubmed.ncbi.nlm.nih.gov/30564206 |
Parent Title (English): | Frontiers in microbiology |
Publisher: | Frontiers Media |
Place of publication: | Lausanne |
Contributor(s): | Chris Greening |
Document Type: | Article |
Language: | English |
Year of Completion: | 2018 |
Date of first Publication: | 2018/12/04 |
Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
Release Date: | 2019/03/05 |
Tag: | CO2 reduction; acetogenesis; clostridia; electron bifurcation; formate dehydrogenase; hydrogen production; hydrogen storage; hydrogenase |
Volume: | 9 |
Issue: | Art. 2911 |
Page Number: | 22 |
First Page: | 1 |
Last Page: | 22 |
Note: | Copyright © 2018 Schuchmann, Chowdhury and Müller. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
HeBIS-PPN: | 448049910 |
Institutes: | Biowissenschaften / Biowissenschaften |
Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
Sammlungen: | Universitätspublikationen |
Open-Access-Publikationsfonds: | Biowissenschaften |
Licence (German): | Creative Commons - Namensnennung 4.0 |