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A biotin‐dependent sodium pump: glutaconyl‐CoA decarboxylase from Acidaminococcus fermentans
Author(s) -
Buckel Wolfgang,
Semmler Roswitha
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)81237-4
Subject(s) - biotin , decarboxylation , chemistry , monensin , avidin , carboxy lyases , sodium , enzyme , biochemistry , organic chemistry , catalysis
The decarboxylation of glutaconyl‐CoA to crotonyl‐CoA in the anaerobic bacterium Acidaminococcus fermentans is catalysed by a membrane‐bound, biotin‐dependent enzyme which requires Na + for activity. Inverted vesicles from A. fermentans accumulated Na + only if glutaconyl‐CoA was decarboxylated. The Na + uptake was inhibited by avidin but not by the avidin biotin complex. Detergents and ionophores such as monensin also prevented the Na + transport. The results indicate that the enzyme is able to convert the free energy of decarboxylation (Δ G o ′ ≈−30 kJ/mol) into a Na + gradient.

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