Literature DB >> 29726568

[FeFe]-Hydrogenases: recent developments and future perspectives.

F Wittkamp1, M Senger, S T Stripp, U-P Apfel.   

Abstract

[FeFe]-Hydrogenases are the most efficient enzymes for catalytic hydrogen turnover. Their H2 production efficiency is hitherto unrivalled. However, functional details of the catalytic machinery and possible modes of application are discussed controversially. The incorporation of synthetically modified cofactors and utilization of semi-artificial enzymes only recently allowed us to shed light on key steps of the catalytic cycle. Herein, we summarize the essential findings regarding the redox chemistry of [FeFe]-hydrogenases and discuss their catalytic hydrogen turnover. We furthermore will give an outlook on potential research activities and exploit the utilization of synthetic cofactor mimics.

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Year:  2018        PMID: 29726568     DOI: 10.1039/c8cc01275j

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN: 1359-7345            Impact factor:   6.222


  9 in total

Review 1.  Biosynthetic Approaches towards the Design of Artificial Hydrogen-Evolution Catalysts.

Authors:  Pallavi Prasad; Dhanashree Selvan; Saumen Chakraborty
Journal:  Chemistry       Date:  2020-08-26       Impact factor: 5.236

2.  Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H2 supports its catalytic relevance.

Authors:  Moritz Senger; Tobias Kernmayr; Marco Lorenzi; Holly J Redman; Gustav Berggren
Journal:  Chem Commun (Camb)       Date:  2022-06-23       Impact factor: 6.065

3.  Geometrical influence on the non-biomimetic heterolytic splitting of H2 by bio-inspired [FeFe]-hydrogenase complexes: a rare example of inverted frustrated Lewis pair based reactivity.

Authors:  Lucile Chatelain; Jean-Baptiste Breton; Federica Arrigoni; Philippe Schollhammer; Giuseppe Zampella
Journal:  Chem Sci       Date:  2022-03-22       Impact factor: 9.969

4.  Spectroscopical Investigations on the Redox Chemistry of [FeFe]-Hydrogenases in the Presence of Carbon Monoxide.

Authors:  Konstantin Laun; Stefan Mebs; Jifu Duan; Florian Wittkamp; Ulf-Peter Apfel; Thomas Happe; Martin Winkler; Michael Haumann; Sven T Stripp
Journal:  Molecules       Date:  2018-07-09       Impact factor: 4.411

5.  Fast Proton Transport in FeFe Hydrogenase via a Flexible Channel and a Proton Hole Mechanism.

Authors:  Rakesh C Puthenkalathil; Bernd Ensing
Journal:  J Phys Chem B       Date:  2022-01-10       Impact factor: 2.991

6.  Insights into Triazolylidene Ligands Behaviour at a Di-Iron Site Related to [FeFe]-Hydrogenases.

Authors:  Andrea Mele; Federica Arrigoni; Catherine Elleouet; François Y Pétillon; Philippe Schollhammer; Giuseppe Zampella
Journal:  Molecules       Date:  2022-07-22       Impact factor: 4.927

7.  Vibrational Perturbation of the [FeFe] Hydrogenase H-Cluster Revealed by 13C2H-ADT Labeling.

Authors:  Vladimir Pelmenschikov; James A Birrell; Leland B Gee; Casseday P Richers; Edward J Reijerse; Hongxin Wang; Simon Arragain; Nakul Mishra; Yoshitaka Yoda; Hiroaki Matsuura; Lei Li; Kenji Tamasaku; Thomas B Rauchfuss; Wolfgang Lubitz; Stephen P Cramer
Journal:  J Am Chem Soc       Date:  2021-05-27       Impact factor: 15.419

8.  Redox-Polymer-Wired [NiFeSe] Hydrogenase Variants with Enhanced O2 Stability for Triple-Protected High-Current-Density H2 -Oxidation Bioanodes.

Authors:  Adrian Ruff; Julian Szczesny; Maria Vega; Sonia Zacarias; Pedro M Matias; Sébastien Gounel; Nicolas Mano; Inês A C Pereira; Wolfgang Schuhmann
Journal:  ChemSusChem       Date:  2020-06-08       Impact factor: 8.928

9.  How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer.

Authors:  Moritz Senger; Viktor Eichmann; Konstantin Laun; Jifu Duan; Florian Wittkamp; Günther Knör; Ulf-Peter Apfel; Thomas Happe; Martin Winkler; Joachim Heberle; Sven Timo Stripp
Journal:  J Am Chem Soc       Date:  2019-10-15       Impact factor: 15.419

  9 in total

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