Interactions among substrates and inhibitors of nitrogenase.
Examination of interactions among various substrates and inhibitors reacting with a partially purified nitrogenase from Azotobacter vinelandii has shown that: nitrous oxide is competitive with N2; carbon monixide and acetylene are noncompetitive with N2; carbon monoxide, cyanide, and nitrous oxide are noncompetitive with acetylene, whereas N2 is competitive with acetylene; carbon monoxide is noncompetitive with cyanide, whereas azide is competitive with cyanide; acetylene and nitrous oxide increase the rate of reduction of cyanide. The results are understandable if nitrogenase serves as an electron sink and substrates and inhibitors bind at multiple modified sites on reduced nitrogenase. It is suggested that substrates such as acetylene may be reduced by a less completely reduced electron sink than is required for the six-electron transfer necessary to reduce N2.
D000114:Acetylene / Q000378:metabolism / Q000494:pharmacology; D001386:Azides / Q000378:metabolism / Q000494:pharmacology; D001395:Azotobacter / Q000201:enzymology; D001665:Binding Sites; D001667:Binding, Competitive; D002248:Carbon Monoxide / Q000494:pharmacology; D003486:Cyanides / Q000378:metabolism; D003864:Depression, Chemical; D006859:Hydrogen / Q000378:metabolism; D007700:Kinetics; D009584:Nitrogen / Q000378:metabolism / Q000494:pharmacology; D009591:Nitrogenase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009609:Nitrous Oxide / Q000494:pharmacology
D001386:Azides; D003486:Cyanides; D002248:Carbon Monoxide; D006859:Hydrogen; D009591:Nitrogenase; D009609:Nitrous Oxide; D009584:Nitrogen; D000114:Acetylene