A5103039757- Metalloenzymes and iron-sulfur proteins
- Electrocatalysts for Energy Conversion
- Metal-Catalyzed Oxygenation Mechanisms
- Advanced battery technologies research
- Enzyme Catalysis and Immobilization
- Catalysis for Biomass Conversion
- Ammonia Synthesis and Nitrogen Reduction
- Catalysis and Hydrodesulfurization Studies
- Advanced Nanomaterials in Catalysis
- Air Quality and Health Impacts
- Medical Imaging and Pathology Studies
- Photosynthetic Processes and Mechanisms
- Hemoglobin structure and function
- Nanocluster Synthesis and Applications
- Corrosion Behavior and Inhibition
- Hydrogen Storage and Materials
- Toxic Organic Pollutants Impact
- Nitric Oxide and Endothelin Effects
- RNA and protein synthesis mechanisms
- CO2 Reduction Techniques and Catalysts
- Occupational and environmental lung diseases
- Carcinogens and Genotoxicity Assessment
- Photoreceptor and optogenetics research
- Cyclone Separators and Fluid Dynamics
- Legume Nitrogen Fixing Symbiosis
Uppsala University
2018-2022
Freie Universität Berlin
2019
Aix-Marseille Université
2010-2017
Centre National de la Recherche Scientifique
2010-2017
Bioénergétique et Ingénierie des Protéines
2009-2016
Boston University
2016
Laboratoire de Chimie Bactérienne
2010-2016
Institut de Microbiologie de la Méditerranée
2009-2015
Délégation Provence et Corse
2015
Goethe University Frankfurt
2010
The mechanism of hydrogen gas formation by [FeFe] hydrogenase is probed under whole cell conditions, revealing the reactive metal hydride species physiologically relevant conditions.
A semi-synthetic screening method for mining the biodiversity of [FeFe]-hydrogenases, expanding toolbox biocatalytic H<sub>2</sub>-gas production.
The Hydrogen Dependent Carbon dioxide Reductase (HDCR) from <italic>Acetobacterium woodii</italic> presents a promising solution to the issue of H<sub>2</sub> storage by reversibly coupling oxidation CO<sub>2</sub> reduction.
Abstract EPR spectroscopy reveals the formation of two different semi‐synthetic hydrogenases in vivo. [FeFe] are metalloenzymes that catalyze interconversion molecular hydrogen and protons. The reaction is catalyzed by H‐cluster, consisting a canonical iron–sulfur cluster an organometallic [2Fe] subsite. It was recently shown enzyme can be reconstituted with synthetic cofactors mimicking composition subsite, resulting hydrogenases. Herein, we employ to monitor such enzymes whole cells. study...
We propose a resolution to the paradox that spectroscopic studies of NiFeSe hydrogenase have not revealed any major signal attributable Ni<sup>III</sup> states formed upon reaction with O<sub>2</sub>, despite fact two inactive are either aerobic or anaerobic oxidation.
Respiratory nitrate reductases (Nars), members of the prokaryotic Mo/W-bis Pyranopterin Guanosine dinucleotide (Mo/W-bisPGD) enzyme superfamily, are key players in respiration, a major bioenergetic pathway widely used by microorganisms to cope with absence dioxygen. The two-electron reduction nitrite takes place at their active site, where molybdenum ion cycles between Mo(VI) and Mo(IV) states via Mo(V) intermediate. site shows two distinct pH-dependent electron paramagnetic resonance (EPR)...
Through the use of an Escherichia coli strain deficient in menaquinone biosynthesis, purified nitrate reductase A (NarGHI)-enriched inner membrane vesicles were titrated and monitored by electron paramagnetic resonance (EPR) spectroscopy, revealing formation protein-bound ubisemiquinone (USQ) species. Two-dimensional ESEEM (HYSCORE) experiments on these radicals revealed same magnetic interaction with 14N nucleus as found for menasemiquinone stabilized at QD site E. NarGHI assigned to His66...
Hydrogenases are metalloenzymes that catalyze the reversible oxidation of molecular hydrogen into protons and electrons. For this purpose, [FeFe]-hydrogenases utilize a hexanuclear iron cofactor, H-cluster. This biologically unique cofactor provides enzyme with outstanding catalytic activities, but it is also highly oxygen sensitive. Under in vitro conditions, stable forms H-cluster denoted H
Abstract [FeFe]-hydrogenase enzymes employ a unique organometallic cofactor for efficient and reversible hydrogen conversion. This so-called H-cluster consists of [4Fe–4S] cubane cysteine linked to diiron complex coordinated by carbon monoxide cyanide ligands an azadithiolate ligand (adt = NH(CH 2 S) )·[FeFe]-hydrogenase apo-protein binding only the sub-complex can be fully activated in vitro addition synthetic site precursor ([2Fe] adt ). Elucidation mechanism assembly will aid design...
Abstract EPR spectroscopy reveals the formation of two different semi‐synthetic hydrogenases in vivo. [FeFe] are metalloenzymes that catalyze interconversion molecular hydrogen and protons. The reaction is catalyzed by H‐cluster, consisting a canonical iron–sulfur cluster an organometallic [2Fe] subsite. It was recently shown enzyme can be reconstituted with synthetic cofactors mimicking composition subsite, resulting hydrogenases. Herein, we employ to monitor such enzymes whole cells. study...
Abstract A major gap of knowledge in metalloproteins is the identity prefolded state protein before cofactor insertion. This holds for molybdoenzymes serving multiple purposes life, especially energy harvesting. large group prokaryotic enzymes allows coordination molybdenum or tungsten cofactors (Mo/W- bis PGD) and Fe/S clusters. Here we report structural data on a cofactor-less enzyme, nitrate reductase respiratory complex characterize conformational changes accompanying Mo/W- PGD...
Hydrogenases are among the fastest H2 evolving catalysts known to date and have been extensively studied under in vitro conditions. Here, we report first mechanistic investigation of an [FeFe]-hydrogenase vivo Functional from green alga Chlamydomonas reinhardtii is generated genetically modified Escherichia coli cells, by addition a synthetic cofactor growth medium. The assembly reactivity resulting semi-synthetic enzyme was monitored using whole-cell electron paramagnetic resonance as well...
Hydrogenases are among the fastest H2 evolving catalysts known to date and have been extensively studied under in vitro conditions. Here, we report first mechanistic investigation of an [FeFe]-hydrogenase vivo Functional from green alga Chlamydomonas reinhardtii is generated genetically modified Escherichia coli cells, by addition a synthetic cofactor growth medium. The assembly reactivity resulting semi-synthetic enzyme was monitored using whole-cell electron paramagnetic resonance as well...