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A bacterial hydrogen‐dependent CO 2 reductase forms filamentous structures
Author(s) -
Schuchmann Kai,
Vonck Janet,
Müller Volker
Publication year - 2016
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13670
Subject(s) - polymerization , enzyme , chemistry , carbon fixation , divalent , formic acid , active site , stereochemistry , biochemistry , organic chemistry , polymer , photosynthesis
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.