Membrane-anchored HDCR nanowires drive hydrogen-powered CO2 fixation

Helge M. Dietrich, Ricardo D. Righetto, Anuj Kumar, Wojciech Wietrzynski, Raphael Trischler, Sandra K. Schuller, Jonathan Wagner, Fabian M. Schwarz, Benjamin D. Engel (), Volker Müller () and Jan M. Schuller ()
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Helge M. Dietrich: Johann Wolfgang Goethe University
Ricardo D. Righetto: Helmholtz Munich
Anuj Kumar: Johann Wolfgang Goethe University
Wojciech Wietrzynski: Helmholtz Munich
Raphael Trischler: Johann Wolfgang Goethe University
Sandra K. Schuller: Philipps-University
Jonathan Wagner: Max Planck Institute of Biochemistry
Fabian M. Schwarz: Johann Wolfgang Goethe University
Benjamin D. Engel: Helmholtz Munich
Volker Müller: Johann Wolfgang Goethe University
Jan M. Schuller: Philipps-University

Nature, 2022, vol. 607, issue 7920, 823-830

Abstract: Abstract 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.

Date: 2022
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DOI: 10.1038/s41586-022-04971-z

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