title: Nitrite, a new substrate for nitrogenase.
abstract: We have examined the reactivity of the purified component proteins of Azotobacter vinelandii nitrogenase (Av1 and Av2) toward nitrate and nitrite. Nitrate has no effect on H2 evolution or C2H2 reduction by nitrogenase and thus is neither a substrate nor an inhibitor. Nitrite dramatically inhibits H2 evolution. This inhibition has two components, one irreversible and one reversible upon addition of CO. The irreversible inhibition is due to nitrite inactivation of the Fe protein. The rate of this inactivation is greatly enhanced by addition of MgATP, suggesting the [4Fe-4S] cluster is the site of nitrite attack. The reversible inhibition does not represent an inhibition of electron flow but rather a diversion of electrons away from H2 evolution and into the six-electron reduction of nitrite to ammonia. Thus, nitrogenase functions as a nitrite reductase.
authors.affiliation: Department of Molecular Biology and Biochemistry, University of California, Irvine 92717.
authors.forename: S A
authors.initials: SA
authors.lastname: Vaughn
authors.forename: B K
authors.initials: BK
authors.lastname: Burgess
mesh_terms: D001395:Azotobacter / Q000201:enzymology*; D007700:Kinetics; D009573:Nitrites / Q000378:metabolism* / Q000494:pharmacology; D009591:Nitrogenase / Q000378:metabolism*; D010084:Oxidation-Reduction; D013379:Substrate Specificity
chemical_list: D009573:Nitrites; D009591:Nitrogenase