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Dietrich, H.M.* ; Righetto, R.D. ; Kumar, A.* ; Wietrzynski, W. ; Trischler, R.* ; Schuller, S.K.* ; Wagner, J.* ; Schwarz, F.M.* ; Engel, B.D. ; Müller, V.* ; Schuller, J.M.*

Membrane-anchored HDCR nanowires drive hydrogen-powered CO2 fixation.

Nature 607, 823-830 (2022)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Filamentous enzymes have been found in all domains of life, but the advantage of filamentation is often elusive1. Some anaerobic, autotrophic bacteria have an unusual filamentous enzyme for CO2 fixation-hydrogen-dependent CO2 reductase (HDCR)2,3-which directly converts H2 and CO2 into formic acid. HDCR reduces CO2 with a higher activity than any other known biological or chemical catalyst4,5, and it has therefore gained considerable interest in two areas of global relevance: hydrogen storage and combating climate change by capturing atmospheric CO2. However, the mechanistic basis of the high catalytic turnover rate of HDCR has remained unknown. Here we use cryo-electron microscopy to reveal the structure of a short HDCR filament from the acetogenic bacterium Thermoanaerobacter kivui. The minimum repeating unit is a hexamer that consists of a formate dehydrogenase (FdhF) and two hydrogenases (HydA2) bound around a central core of hydrogenase Fe-S subunits, one HycB3 and two HycB4. These small bacterial polyferredoxin-like proteins oligomerize through their C-terminal helices to form the backbone of the filament. By combining structure-directed mutagenesis with enzymatic analysis, we show that filamentation and rapid electron transfer through the filament enhance the activity of HDCR. To investigate the structure of HDCR in situ, we imaged T. kivui cells with cryo-electron tomography and found that HDCR filaments bundle into large ring-shaped superstructures attached to the plasma membrane. This supramolecular organization may further enhance the stability and connectivity of HDCR to form a specialized metabolic subcompartment within the cell.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Sprache englisch
Veröffentlichungsjahr 2022
HGF-Berichtsjahr 2022
ISSN (print) / ISBN 0028-0836
e-ISSN 1476-4687
Zeitschrift Nature
Quellenangaben Band: 607, Heft: 7920, Seiten: 823-830 Artikelnummer: , Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Begutachtungsstatus Peer reviewed
Institut(e) Helmholtz Pioneer Campus (HPC)
POF Topic(s) 30203 - Molecular Targets and Therapies
Forschungsfeld(er) Pioneer Campus
PSP-Element(e) G-510008-001
Förderungen European Research Council
Universität Basel
Deutsche Bundesstiftung Umwelt
Alexander von Humboldt-Stiftung
European Molecular Biology Organization
Max Planck Institute for Biochemistry computing cluster in Martinsried
Helmholtz Munich
Deutsche Forschungsgemeinschaft
DOI 10.1038/s41586-022-04971-z
WOS ID WOS:000828280500001
Scopus ID 85134470429
PubMed ID 35859174
Erfassungsdatum 2022-11-03
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