Reduction of azide by the N2-fixing enzyme system.
- 1 May 1967
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 57 (5) , 1317-1323
- https://doi.org/10.1073/pnas.57.5.1317
Abstract
Cell-free N2-fixing enzyme preparations from Clostridium pasteurianum did not reduce the N-N bond of hydrazine or of some of its derivatives; the compounds were only weak inhibitors of N2 fixation. Diazo compounds were not reduced, but p-diazobenzenesulfonic acid strongly inhibited N2 fixation. Azide was reduced to N2 and NH3 by the extracts. Azide reduction, like N2 fixation, requires an electron donor and an ATP source. It is inhibited by CO, nitric oxide, acetylene and nitroprusside. Azide is reduced at the same site as N2. Preparations of Azotobacter vine-landii capable of fixing N2 which also reduce azide to NH3 and N2 and require an electron donor and ATP; do not reduce hydrazine.This publication has 12 references indexed in Scilit:
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