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Nitrite, a new substrate for nitrogenase

Journal Article · · Biochemistry; (USA)
DOI:https://doi.org/10.1021/bi00428a002· OSTI ID:5512705
;  [1]
  1. Univ. of California, Irvine (USA)
The authors 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 H{sub 2} evolution or C{sub 2}H{sub 2} reduction by nitrogenase and thus is neither a substrate nor an inhibitor. Nitrite dramatically inhibits H{sub 2} 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 H{sub 2} evolution and into the six-electron reduction of nitrite to ammonia. Thus, nitrogenase functions as a nitrite reductase.
OSTI ID:
5512705
Journal Information:
Biochemistry; (USA), Journal Name: Biochemistry; (USA) Vol. 28:2; ISSN 0006-2960; ISSN BICHA
Country of Publication:
United States
Language:
English