In nature, hydrogenase enzymes mediate production and consumption of hydrogen (H2). However, hydrogenases are very sensitive to oxygen (O2) and heat, which restricts their use in technology. Now scientists from Seigo Shima`s group have successfully solved the crystal structure of [Fe]-hydrogenase in its activated form, thus providing chemists with indispensable information for designing robust and powerful H2 catalysts.

And … Action!
Atomic crystal structure of activated [Fe]-hydrogenase resolved

In nature, hydrogenase enzymes mediate production and consumption of hydrogen (H2). However, hydrogenases are very sensitive to oxygen (O2) and heat, which restricts their use in technology. Now scientists from Seigo Shima`s group have successfully solved the crystal structure of [Fe]-hydrogenase in its activated form, thus providing chemists with indispensable information for designing robust and powerful H2 catalysts.

Hydrogen gas (H2) is proposed as a clean energy carrier for the future world - as long as its production works without the use of fossil fuels. Accordingly, there is intensive research on hydrogenases, enzymes that catalyze H2 production and consumption. Now scientists from MPI’s Shima group in cooperation with scientists from Lausanne were able to construct an active semisynthetic [Mn]-hydrogenase, thus providing a new way for designing and building new robust and efficient H2-activtion catalysts that might take part in future technologies.

[Mn]-hydrogenase: A new step towards redesigning hydrogenases

Hydrogen gas (H2) is proposed as a clean energy carrier for the future world - as long as its production works without the use of fossil fuels. Accordingly, there is intensive research on hydrogenases, enzymes that catalyze H2 production and consumption. Now scientists from MPI’s Shima group in cooperation with scientists from Lausanne were able to construct an active semisynthetic [Mn]-hydrogenase, thus providing a new way for designing and building new robust and efficient H2-activtion catalysts that might take part in future technologies.
On May 29, Angela Dorn, Hessian Minister of State for Science and the Arts, and Dr. Ulrike Mattig, Head of Department for Non-University Research Institutions, visited the Max Planck Institute for Terrestrial Microbiology at the Lahnbergen in Marburg.

Hesse's Science Minister Angela Dorn visits the Max Planck Institute for Terrestrial Microbiology

On May 29, Angela Dorn, Hessian Minister of State for Science and the Arts, and Dr. Ulrike Mattig, Head of Department for Non-University Research Institutions, visited the Max Planck Institute for Terrestrial Microbiology at the Lahnbergen in Marburg.

Everyone who follows the Formula 1 knows that securing the pole position is not simple. The same is true for many proteins in rod-shaped bacteria like Myxococcus xanthus: for enabling gliding movement, they must localize to the cell poles. In a recent publication in Nature Microbiology, scientists from the Max Planck Institute for Terrestrial Microbiology together with scientists from the Technical University in Munich unraveled a novel mechanism of bacterial movement.

It`s all about the Pole Position

Everyone who follows the Formula 1 knows that securing the pole position is not simple. The same is true for many proteins in rod-shaped bacteria like Myxococcus xanthus: for enabling gliding movement, they must localize to the cell poles. In a recent publication in Nature Microbiology, scientists from the Max Planck Institute for Terrestrial Microbiology together with scientists from the Technical University in Munich unraveled a novel mechanism of bacterial movement.
In cooperation with scientists in Frankfurt and Berlin, Max Planck researchers from Marburg have discovered that bacteria are also able to produce the [Fe]-hydrogenase HmdII and the FeGP cofactor. Their results are of great importance for the biotechnological development of [Fe]-hydrogenase variants that also function in bacteria.

Discovery of [Fe]-hydrogenase in bacteria opens new possibilities for conversion of hydrogen

In cooperation with scientists in Frankfurt and Berlin, Max Planck researchers from Marburg have discovered that bacteria are also able to produce the [Fe]-hydrogenase HmdII and the FeGP cofactor. Their results are of great importance for the biotechnological development of [Fe]-hydrogenase variants that also function in bacteria.
June 2019
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Prof. Dr. Ruedi Aebersold

at 14:15

Mass spectrometric exploration of the proteotype

Dr. Norio Takeshita

at 13:00

Fungal-bacterial mutualistic interaction; fungal highway and bacterial toll

Prof. Dr. Christoph Haselwandter

at 11:00

Mechanosensing in cell membranes

Marian Breuer

at 16:00

Computational modeling of metabolism in a minimal cell

Dr. Marie-Eve Kennedy-Val

at 16:15

Replication control of multiple chromosomes in bacteria

Postponed to 16:15 h

Dr. Patricia C. Dos Santos

at 13:15

Sulfur incorporation into tRNA: Unique mechanistic features and functions in bacteria

next Seminars & Events

Prof. Dr. Ralf Koebnik

What would be a microbe’s life without SWEETs: TALEs from Xanthomonas
Jul 2, 2019 13:15
MPI for Terrestrial Microbiology, Room: Lecture hall

Dr. Patrick Yizhi Cai

Synthetic genomics: from genetic parts to genomes
Jul 8, 2019 13:15
MPI for Terrestrial Microbiology, Room: Lecture hall

Cesar Sanchez

How to get published in Nature Communications and other Nature journals
Jul 9, 2019 13:00
MPI for Terrestrial Microbiology, Room: Lecture hall

Gita Naseri

Plant-derived regulators and their application in COMPASS optimization method
Jul 9, 2019 14:00
MPI for Terrestrial Microbiology, Room: Seminar Room

Prof. Dr. Sven Krappmann

Protecting the offspring – Linking developmental pathways of Aspergillus fumigatus to toxic compounds
Jul 15, 2019 13:15
MPI for Terrestrial Microbiology, Room: Lecture hall
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