Abstract
Among organic compounds tested for their ability to support nitrogenase activity in isolated heterocysts of Anabaena sp. strain 7120 under argon, D-erythrose (5 mM) was unique in supporting acetylene reduction at 10 times the control rates. Higher concentrations of D-erythrose exhibited substrate inhibition. At 50 kPa of H2, all concentrations of D-erythrose inhibited H2-supported acetylene reduction. The effects of D-erythrose on nitrogenase activity were explored. Erythrose enhanced 15N2 incorporation by heterocysts, but NADP+ did not enhance erythrose-supported acetylene reduction. H2 protected nitrogenase from O2 inactivation, but erythrose did not; erythrose did not counter protection by H2. Tests with inhibitors of electron transport showed that erythrose-supported acetylene reduction requires electron flow through ferredoxin, a b-type cytochrome, and a 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone-sensitive transfer agent whose electron flow is not mediated through the plastoquinone and Rieske iron protein.
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Dates
Type | When |
---|---|
Created | 5 years, 8 months ago (Jan. 3, 2020, 12:55 p.m.) |
Deposited | 4 years, 1 month ago (July 29, 2021, 1:33 p.m.) |
Indexed | 1 year, 2 months ago (June 16, 2024, 7:34 p.m.) |
Issued | 41 years, 7 months ago (Feb. 1, 1984) |
Published | 41 years, 7 months ago (Feb. 1, 1984) |
Published Print | 41 years, 7 months ago (Feb. 1, 1984) |
@article{Privalle_1984, title={D-erythrose supports nitrogenase activity in isolated Anabaena sp. strain 7120 heterocysts}, volume={157}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.157.2.350-356.1984}, DOI={10.1128/jb.157.2.350-356.1984}, number={2}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Privalle, L S and Burris, R H}, year={1984}, month=feb, pages={350–356} }