![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.](/523888/original-1560942340.png?t=eyJ3aWR0aCI6MTUxMCwiaGVpZ2h0Ijo4NDksImZpdCI6ImNyb3AiLCJvYmpfaWQiOjUyMzg4OH0=--63a9b77233eb425385144a88679231d640a6dbb9)
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.](/523934/original-1560940580.png?t=eyJ3aWR0aCI6MTUxMCwiaGVpZ2h0Ijo4NDksImZpdCI6ImNyb3AiLCJvYmpfaWQiOjUyMzkzNH0=--9c9dec8aee8bd14be07de9f1853b4f5ac81c16f3)
[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.
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.
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.](/523911/original-1558295812.png?t=eyJ3aWR0aCI6MTUxMCwiaGVpZ2h0Ijo4NDksImZpdCI6ImNyb3AiLCJvYmpfaWQiOjUyMzkxMX0=--6bb3e1dc5d66048d3f57f41ab2958d30b9acee2c)
