Johannes G. Rebelein

Farming and climate legacies shape the seed microbiota and offspring drought responses in wheat

B.C. Sharma, Josephine Burgmans, Niels N. Oehlmann, Johannes G. Rebelein et autres

Abstract Seeds link parental environments to offspring establishment, but whether seed-associated bacteria retain signatures of farming and climate legacies across plant generations remains unclear. Here, we characterized epiphytic and endophytic bacterial communities of winter wheat seeds collected from the Global Change Experimental …

de (code pays fourni par la source)

Directed evolution of the Fe-nitrogenase for CO 2 reduction to hydrocarbons

Niels N. Oehlmann, Frederik V. Schmidt, Jing Chen, Simone Prinz et autres

Abstract The iron (Fe) nitrogenase drives bacterial methane (CH 4 ) formation by converting carbon dioxide (CO 2 ) to CH 4 in a single enzymatic step. Enhancing the initial CH 4 formation activity of Fe-nitrogenase and expanding the product spectrum to …

de (code pays fourni par la source)

Functional insights into the nitrogenase-like enzyme superfamily

Ana Lago-Maciel, Marcello Herzog, Johannes G. Rebelein

Nitrogenases are the only enzymes capable of converting atmospheric nitrogen into bioavailable ammonia, an essential process for all life on Earth. Early ancestors of bona fide nitrogenases and their maturases gave rise to several structural homologues with diverse functions. The nitrogen fixation-like …

de (code pays fourni par la source)

Methylthio-alkane reductases use nitrogenase metalloclusters for carbon–sulfur bond cleavage

Ana Lago-Maciel, Jéssica C. Soares, Jan Zarzycki, Charles Buchanan et autres

Abstract Methylthio-alkane reductases convert methylated sulfur compounds to methanethiol and small hydrocarbons, a process with important environmental and biotechnological implications. These enzymes are classified as nitrogenase-like enzymes, despite lacking the ability to convert dinitrogen to ammonia, raising fundamental questions about the factors …

de, gb (code pays fourni par la source)

Alternative Substrates of Nitrogenase

Frederik V. Schmidt, Johannes G. Rebelein

Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia, a reaction vital to all life on Earth. To catalyze this challenging reaction, nitrogenases rely on complex metallocofactors at their active site, which can reduce a wide range of alternative …

de (code pays fourni par la source)

NAD-dependent dehydrogenases enable efficient growth of Paracoccus denitrificans on the PET monomer ethylene glycol

Minrui Ren, Holly Addison, Willem E. M. Noteborn, Elisabeth H Andeweg et autres

Ethylene glycol is a monomer of the plastic polyethylene terephthalate (PET) and an environmental pollutant of increasing concern. Although it is generally accepted that bacteria use ethylene glycol as growth substrate, not all involved enzymes are well understood. Here, we show that …

nl, de (code pays fourni par la source)

Two Key Ferredoxins for Nitrogen Fixation Have Different Specificities and Biophysical Properties

Holly Addison, Pascal Pfister, Ana Lago-Maciel, Tobias J. Erb et autres

Abstract Ferredoxins deliver electrons to drive many challenging biochemical transformations, including enzyme‐catalyzed nitrogen fixation. We recently showed two distinct ferredoxins, FdC and FdN, were essential for iron nitrogenase‐mediated nitrogen fixation in R. capsulatus . In this study, we perform investigations on FdC …

de (code pays fourni par la source)

Investigation of ethylene glycol metabolism in Paracoccus denitrificans

Meng Ren, Holly Addison, Elisabeth H Andeweg, Willem E. M. Noteborn et autres

de, nl (code pays fourni par la source)

EuChemS‐Nachwuchsworkshop in Galway

Johannes G. Rebelein, Franziska Traube

Abstract Zum vierten Young Investigator Workshop (YIW) der EuChemS Chemistry for Life Science Division trafen sich vom 12. bis 13. Juli 2024 in Galway vierzehn Nachwuchsgruppenleiterinnen und ‐leiter aus ganz Europa, die zu chemischer Biologie forschen.

Methylthio-alkane reductases use nitrogenase metalloclusters for carbon-sulfur bond cleavage

Ana Lago-Maciel, Jéssica C. Soares, Jan Zarzycki, Charles Buchanan et autres

Abstract Methylthio-alkane reductases convert methylated sulfur compounds to methanethiol and small hydrocarbons, a process with important environmental and biotechnological implications. These enzymes are classified as nitrogenase-like enzymes, despite lacking the ability to convert dinitrogen to ammonia, raising fundamental questions about the factors …

de, ch, gb (code pays fourni par la source)

Generating Site Saturation Mutagenesis Libraries and Transferring Them to Broad Host-Range Plasmids Using Golden Gate Cloning

Niels N. Oehlmann, Johannes G. Rebelein

de (code pays fourni par la source)

The iron nitrogenase reduces carbon dioxide to formate and methane under physiological conditions: A route to feedstock chemicals

Niels N. Oehlmann, Frederik V. Schmidt, Marcello Herzog, Annelise L. Goldman et autres

Nitrogenases are the only known enzymes that reduce molecular nitrogen (N 2 ) to ammonia. Recent findings have demonstrated that nitrogenases also reduce the greenhouse gas carbon dioxide (CO 2 ), suggesting CO 2 to be a competitor of N 2 . …

de (code pays fourni par la source)