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Inhibition of nitrogenase by nitrite and nitric oxide inRhodopseudomonas sphaeroidesf. sp.denitrificans

โœ Scribed by W. P. Michalski; D. J. D. Nicholas

Publisher
Springer
Year
1987
Tongue
English
Weight
490 KB
Volume
147
Category
Article
ISSN
0302-8933

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โœฆ Synopsis

In cells of Rhodopseudomonas sphaeroides f. sp. denitrifieans nitrite and nitric oxide, the products of denitrification, inhibit activity of nitrogenase enzyme.

Ferredoxin-linked COz fixation, with H2 as a reductant, was also inhibited by nitrite and NO in denitrifying cells.

EPR spectroscopy of cell preparations treated with NO showed that it reacts with non-haem iron-sulphur proteins to form iron-nitrosyl complexes. Nitrite also reacts with these iron-sulphur proteins, but the formation of ironnitrosyl complexes was dependent on the presence of dithionite. Since nitrite is reduced to NO by dithionite it is likely that nitrogenase and CO2 fixation reactions are inhibited not only by nitrite itself, but also by nitric oxide.

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