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Title | A bacterial tungsten-containing aldehyde oxidoreductase forms an enzymatic decorated protein nanowire. |
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Journal, issue, pages | Sci Adv, Vol. 9, Issue 22, Page eadg6689, Year 2023 |
Publish date | Jun 2, 2023 |
Authors | Agnieszka Winiarska / Fidel Ramírez-Amador / Dominik Hege / Yvonne Gemmecker / Simone Prinz / Georg Hochberg / Johann Heider / Maciej Szaleniec / Jan Michael Schuller / |
PubMed Abstract | 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 ...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 (AOR) 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. |
External links | Sci Adv / PubMed:37267359 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.22 Å |
Structure data | EMDB-16376, PDB-8c0z: |
Chemicals | ChemComp-SF4: ChemComp-T7R: ChemComp-MG: ChemComp-BEZ: ChemComp-FAD: |
Source |
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Keywords | OXIDOREDUCTASE / Tungsten-containing enzyme / nanowires. |