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• W2334272185 endingPage "1322" @default.
• W2334272185 startingPage "1311" @default.
• W2334272185 abstract "Interconversion of CO 2 and formic acid is an important reaction in bacteria. A novel enzyme complex that directly utilizes molecular hydrogen as electron donor for the reversible reduction of CO 2 has recently been identified in the Wood–Ljungdahl pathway of an acetogenic bacterium. This pathway is utilized for carbon fixation as well as energy conservation. Here we describe the further characterization of the quaternary structure of this enzyme complex and the unexpected behavior of this enzyme in polymerizing into filamentous structures. Polymerization of metabolic enzymes into similar structures has been observed only in rare cases but the increasing number of examples point towards a more general characteristic of enzyme functioning. Polymerization of the purified enzyme into ordered filaments of more than 0.1 μm in length was only dependent on the presence of divalent cations. Polymerization was a reversible process and connected to the enzymatic activity of the oxygen‐sensitive enzyme with the filamentous form being the most active state." @default.
• W2334272185 created "2016-06-24" @default.
• W2334272185 creator A5000745618 @default.
• W2334272185 creator A5006690483 @default.
• W2334272185 creator A5061802621 @default.
• W2334272185 date "2016-02-19" @default.
• W2334272185 modified "2023-10-15" @default.
• W2334272185 title "A bacterial hydrogen-dependent CO₂reductase forms filamentous structures" @default.
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• W2334272185 doi "https://doi.org/10.1111/febs.13670" @default.
• W2334272185 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26833643" @default.
• W2334272185 hasPublicationYear "2016" @default.
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