Membrane-anchored HDCR nanowires drive hydrogen-powered CO2 fixation

Dietrich, Helge M.; Righetto, Ricardo D.; Kumar, Anuj; Wietrzyñski, Wojciech; Trischler, Raphael; Schuller, Sandra K.; Wagner, Jonathan; Schwarz, Fabian; Engel, Benjamin D.; Müller, Volker; Schuller, Jan M.

doi:10.1038/s41586-022-04971-z

Cited by 47 publications

(65 citation statements)

References 81 publications

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“…The polymerized enzyme exhibited higher activity than the monomeric fraction of the enzyme (31,32). A similar phenomenon has been observed for the bifunctional CoA-dependent acetaldehyde and alcohol dehydrogenase AdhE of Escherichia coli (30,33) and the HDCR, a key enzyme of the acetogenic metabolism of Acetobacterium woodii (30) and Thermoanaerobacter kivui (20).…”

Section: Discussionsupporting

confidence: 76%

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

et al. 2023

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Aldehyde oxidoreductases (AORs) are tungsten enzymes catalyzing the oxidation of many different aldehydes to the corresponding carboxylic acids. In contrast to other known AORs, the enzyme from the denitrifying betaproteobacterium Aromatoleum aromaticum (AOR Aa ) consists of three different subunits (AorABC) and uses nicotinamide adenine dinucleotide (NAD) as an electron acceptor. Here, we reveal that the enzyme forms filaments of repeating AorAB protomers that are capped by a single NAD-binding AorC subunit, based on solving its structure via cryo–electron microscopy. The polyferredoxin-like subunit AorA oligomerizes to an electron-conducting nanowire that is decorated with enzymatically active and W-cofactor (W-co) containing AorB subunits. Our structure further reveals the binding mode of the native substrate benzoate in the AorB active site. This, together with quantum mechanics:molecular mechanics (QM:MM)–based modeling for the coordination of the W-co, enables formulation of a hypothetical catalytic mechanism that paves the way to further engineering for applications in synthetic biology and biotechnology.

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Section: Discussionsupporting

confidence: 76%

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

et al. 2023

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“…A unique feature of AorA is the structure of the C-terminal twenty amino acids, which are highly conserved in the sequences of the AOR Aa subclade members but not in any other related sequence. These residues form an α-helix protruding from the ferredoxin fold, which resembles similar structures known from filament-forming redox proteins, such as HDCR ( 19 ). This C-terminal helix of AorA provides an additional surface to extend the interface with the next AorA subunit in the oligomer, probably facilitating filament formation by hydrogen bridges and hydrophobic interactions (Fig.…”

Section: Resultsmentioning

confidence: 82%

“…The polymerised enzyme exhibited higher activity than the monomeric fraction of enzyme ( 30, 31 ) A similar phenomenon has been observed for the bifunctional CoA-dependent acetaldehyde and alcohol dehydrogenase AdhE of E. coli ( 29, 32 ) and the hydrogen-dependent CO 2 reductase (HDCR), a key enzyme of the acetogenic metabolism of Acetobacterium woodii ( 29 ). and Thermoanaerobacter kivui ( 19 ).…”

Section: Discussionmentioning

confidence: 99%

“…Similar to AOR Aa , filamentation of HDCR is mediated by the C-terminal helices from the two polyferredoxin subunits HycB3 and HycB4, which in both cases was proven by site-directed mutagenesis. These two subunits form the core of a nanofilament and bind enzymatically active counterparts ( 19 ). However, neither HycB3 nor HycB4 are orthologous to AorA, although they present a similar overall structure: all three subunits consist of two fused bacterial ferredoxin domains which superimpose well structurally (RMSD 3.62, Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Unexpectedly, our structure reveals that an extended protein filament is formed by AorAB protomers that is nucleated by a single FAD-containing AorC subunit. The repeating units are connected through a poly-ferredoxin chain generated by lined-up ferredoxin-like AorA subunits, essentially forming an electron-conducting “nanowire” decorated with enzymatically active W-cofactor (W-co) containing AorB subunits, reminiscent of another recently characterised polymer-forming redox enzyme, the hydrogen-dependent CO 2 -reductase (HDCR) ( 19 ). This novel form of redox-enzyme has the potential to stabilize the complex as well as to link enzymatic subunits through the filament to increase their catalytic activity.…”

Section: Introductionmentioning

confidence: 99%

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A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

Winiarska

Ramírez-Amador

Hege

et al. 2023

Preprint

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Aldehyde oxidoreductases (AOR) are tungsten enzymes catalysing the oxidation of many different aldehydes to the corresponding carboxylic acids. In contrast to other known AORs, the enzyme from the denitrifying betaproteobacteriumAromatoleum aromaticum(AORAa) consists of three different subunits (AorABC) and utilizes NAD as electron acceptor. Here we reveal that the enzyme forms filaments of repeating AorAB protomers which are capped by a single NAD-binding AorC subunit, based on solving its structure via cryo-electron microscopy. The polyferredoxin-like subunit AorA oligomerizes to an electron-conducting nanowire that is decorated with enzymatically active and W-cofactor (W-co) containing AorB subunits. Our structure further reveals the binding mode of the native substrate benzoate in the AorB active site. This, together with QM:MM-based modelling for the coordination of the W-co, enables formulation of catalytic mechanism hypothesis that paves the way for further engineering of AOR for applications in synthetic biology and biotechnology.

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Super‐fast Charging Biohybrid Batteries through a Power‐to‐formate‐to‐bioelectricity Process by Combining Microbial Electrochemistry and CO₂ Electrolysis

Chu,

Jiang,

Wang

et al. 2023

Angewandte Chemie

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Extensive study on renewable energy storage has been sparked by the growing worries regarding global warming. In this study, incorporating the latest advancements in microbial electrochemistry and electrochemical CO2 reduction, a super‐fast charging biohybrid battery was introduced by using pure formic acid as an energy carrier. CO2 electrolyser with a slim‐catholyte layer and a solid electrolyte layer was built, which made it possible to use affordable anion exchange membranes and electrocatalysts that are readily accessible. The biohybrid battery only required a 3‐minute charging to accomplish an astounding 25‐hour discharging phase. In the power‐to‐formate‐to‐bioelectricity process, bioconversion played a vital role in restricting both the overall Faradaic efficiency and Energy efficiency.The CO2 electrolyser was able to operate continuously for an impressive total duration of 164 hours under Gas Stand‐By model, by storing N2 gas in the extraction chamber during stand‐by periods. Additionally, the electric signal generated during the discharging phase was utilized for monitoring water biotoxicity. Functional genes related to formate metabolism were identified in the bioanode and electrochemically active bacteria were discovered. On the other hand, Paracoccus was predominantly found in the used air cathode. These results advance our current knowledge of exploiting biohybrid technology.

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Membrane-anchored HDCR nanowires drive hydrogen-powered CO2 fixation

Cited by 47 publications

References 81 publications

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

Super‐fast Charging Biohybrid Batteries through a Power‐to‐formate‐to‐bioelectricity Process by Combining Microbial Electrochemistry and CO₂ Electrolysis

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Membrane-anchored HDCR nanowires drive hydrogen-powered CO2 fixation

Cited by 47 publications

References 81 publications

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire

Super‐fast Charging Biohybrid Batteries through a Power‐to‐formate‐to‐bioelectricity Process by Combining Microbial Electrochemistry and CO2 Electrolysis

Contact Info

Product

Resources

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Super‐fast Charging Biohybrid Batteries through a Power‐to‐formate‐to‐bioelectricity Process by Combining Microbial Electrochemistry and CO₂ Electrolysis