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Showing 1–15 of 15 results
Advanced filters: Author: Jan Zarzycki Clear advanced filters

  • Methylthio-alkane reductases are recently discovered enzymes that can produce methanethiol and small hydrocarbons from methylated sulfur compounds. Now the cryo-EM structure of a methylthio-alkane reductase complex is solved, revealing large metalloclusters previously observed only within nitrogenases.

    • Ana Lago-Maciel
    • Jéssica C. Soares
    • Johannes G. Rebelein
    ResearchOpen Access
    Nature Catalysis
    Volume: 8, P: 1086-1099

  • Biological CO2 fixation is restricted to few enzymes and pathways, limiting its value in environmental protection and agricultural productivity. Now, a new-to-nature CO2-fixing enzyme allows CO2-dependent assimilation of glycolate in a designed pathway, and its use for different applications is demonstrated.

    • Marieke Scheffen
    • Daniel G. Marchal
    • Tobias J. Erb
    ResearchOpen Access
    Nature Catalysis
    Volume: 4, P: 105-115

  • Available enzymatic CO2 reduction strategies are not suitable for aerobic microorganisms and many industrial settings. Here, the authors design a new metabolic pathway that can operate under fully aerobic conditions, ambient CO2 levels, and seamlessly integrate with well-established C1-assimilation pathways.

    • Ari Satanowski
    • Daniel G. Marchal
    • Tobias J. Erb
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-18

  • Enzyme promiscuity seeds evolutionary innovation, but how flexible a single enzyme can be (re-)used during evolution remains unclear. Here, the authors show that various evolutionary trajectories applied to succinate semialdehyde dehydrogenase can compensate for the loss of two different functions in E. coli.

    • Hai He
    • Paul A. Gómez-Coronado
    • Tobias J. Erb
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-15

  • Prokaryotic cell transcriptomics has been limited to mixed or sub-population dynamics and individual cells within heterogeneous populations. Here the authors develop a ‘TRANSITomic’ approach to profile transcriptomes of single Burkholderia pseudomallei cells as they transit through host cell infection.

    • Yun Heacock-Kang
    • Ian A. McMillan
    • Tung T. Hoang
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-12

  • Using cryo-EM, Schmidt, Schulz, et al. solve the structure of the iron nitrogenase complex, which shows a unique architecture of alternative nitrogenases and suggests the G subunit to be involved in substrate channeling, stabilization of the cofactor and determining specificty among nitrogenase components.

    • Frederik V. Schmidt
    • Luca Schulz
    • Johannes G. Rebelein
    ResearchOpen Access
    Nature Structural & Molecular Biology
    Volume: 31, P: 150-158

  • A key step in the assimilation of formate is its reduction into formaldehyde. Here, the authors develop a two-enzyme route in which formate is activated into formyl phosphate and reduced by NAD(P)H into formaldehyde and confirm its functionality in vitro and in vivo.

    • Maren Nattermann
    • Sebastian Wenk
    • Tobias J. Erb
    ResearchOpen Access
    Nature Communications
    Volume: 14, P: 1-14

  • Marine Proteobacteria use the β-hydroxyaspartate cycle to assimilate glycolate, which is secreted by algae on a petagram scale, providing evidence of a previously undescribed trophic interaction between autotrophic phytoplankton and heterotrophic bacterioplankton.

    • Lennart Schada von Borzyskowski
    • Francesca Severi
    • Tobias J. Erb
    Research
    Nature
    Volume: 575, P: 500-504

  • Structural and biochemical analysis of propionyl-CoA synthase reveals that it forms a reaction chamber containing three active sites, which sequesters the reactive intermediate acrylyl-CoA during the conversion of 3-hydroxypropionate to propionyl-CoA.

    • Iria Bernhardsgrütter
    • Bastian Vögeli
    • Tobias J. Erb
    Research
    Nature Chemical Biology
    Volume: 14, P: 1127-1132

  • The cryo-electron microscopy structure of the filamentous hydrogen-dependent CO2 reductase (HDCR) enzyme from Thermoanaerobacter kivui, together with enzymatic analysis and in situ cryo-electron tomography, provides insight into the high catalytic activity of HDCR.

    • Helge M. Dietrich
    • Ricardo D. Righetto
    • Jan M. Schuller
    Research
    Nature
    Volume: 607, P: 823-830

  • To date, three different autotrophic carbon fixation mechanisms have been found in archaea. Here, Georg Fuchs and colleagues describe these mechanisms and their phylogenetic distribution. As most cultivated autotrophic archaea live in conditions that resemble the conditions of early life, these pathways can serve as models for an ancestral autotrophic carbon fixation pathway.

    • Ivan A. Berg
    • Daniel Kockelkorn
    • Georg Fuchs
    Reviews
    Nature Reviews Microbiology
    Volume: 8, P: 447-460

  • Bacterial microcompartments are self-assembling organelles that consist of an enzymatic core that is encapsulated by a selectively permeable protein shell. In this Review, Kerfeld and colleagues discuss recent insights into the structure, assembly, diversity and function of bacterial microcompartments.

    • Cheryl A. Kerfeld
    • Clement Aussignargues
    • Markus Sutter
    Reviews
    Nature Reviews Microbiology
    Volume: 16, P: 277-290