| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Caserta, Giorgio
Technische Universität Berlin
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (7/7 displayed)
- 2023Substrate-Gated Transformation of a Pre-Catalyst into an Iron-Hydride Intermediate [(NO)2(CO)Fe(μ-H)Fe(CO)(NO)2]- for Catalytic Dehydrogenation of Dimethylamine Boranecitations
- 2023Substrate-Gated Transformation of a Pre-Catalyst into an Iron-Hydride Intermediate [(NO)$_2$ (CO)Fe(μ-H)Fe(CO)(NO)$_2$]$^−$ for Catalytic Dehydrogenation of Dimethylamine Boranecitations
- 2022Exploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes
- 2021Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies
- 2021Exploring structure and function of redox intermediates of [NiFe]-hydrogenases by an advanced experimental approach for solvated, lyophilized and crystallized metalloenzymes.citations
- 2021Exploring Structure and Function of Redox Intermediates in [NiFe]-Hydrogenases by an Advanced Experimental Approach for Solvated, Lyophilized and Crystallized Metalloenzymes
- 2018Fully electrochemical MIP sensor for artemisinincitations
Places of action
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article
Exploring structure and function of redox intermediates of [NiFe]-hydrogenases by an advanced experimental approach for solvated, lyophilized and crystallized metalloenzymes.
Abstract
A profound mechanistic characterization of complex metalloenzymes requires a multitude of complementary techniques. In this context, we developed a new experimental setup allowing controlled preparation of catalytic intermediates for characterization by various spectroscopic techniques. The in situ monitoring of redox transitions by infrared spectroscopy in enzyme lyophilizate, crystals and solution during gas exchange in a wide temperature range can be accomplished as well. As a proof of concept, two O 2 -tolerant [NiFe]-hydrogenases were investigated as model systems. First, we utilized our platform to prepare highly concentrated hydrogenase lyophilizate in a paramagnetic state harboring a bridging hydride. This procedure proved beneficial for 57 Fe nuclear resonance vibrational spectroscopy and revealed, in combination with density functional theory calculations, the vibrational fingerprint of this catalytic intermediate. Furthermore, in combination with resonance Raman spectroscopy, the same in situ IR setup provided detailed insights into the redox chemistry of enzyme crystals, underlining the general necessity to complement X-ray crystallographic data with spectroscopic analyses.