A bacterial hydrogen-dependent CO2 reductase forms filamentous structures

The FEBS Journal
Kai SchuchmannVolker Müller

Abstract

Interconversion of CO2 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 CO2 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.

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Citations

Sep 15, 2016·Extremophiles : Life Under Extreme Conditions·Mirko Basen, Volker Müller
Mar 6, 2018·Preparative Biochemistry & Biotechnology·M Mervan ÇakarBarış Binay
Jun 18, 2017·Biochemical Society Transactions·Abulikemu AbudukelimuHans V Westerhoff
Sep 7, 2018·Biotechnology for Biofuels·Fabian M SchwarzVolker Müller
Dec 30, 2020·Proceedings of the National Academy of Sciences of the United States of America·Matthew JessopIrina Gutsche
Jun 9, 2021·The Protein Journal·Aişe ÜnlüBarış Binay

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