Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Feb;70(2):339–342. doi: 10.1073/pnas.70.2.339

Reduction of Acetylene and Hydrazine with a Molybdenum-Glutathione Complex

Dietrich Werner 1,*, Sterling A Russell 1, Harold J Evans 1
PMCID: PMC433253  PMID: 16592055

Abstract

Crystalline preparations of a molybdenum-glutathione complex catalyze the reduction of acetylene to ethylene in the presence of borohydride. The reaction proceeds at rates up to 6 mol of C2H2 produced per min per mol of bound Mo, which is 4% of the activity of a quantity of nitrogenase with an equivalent amount of Mo. The activity of the complex is enhanced 100-fold by ATP, but the addition of ADP has no effect. Stimulation in activity by GTP is about the same as that by ATP, and the effects of CTP or UTP are considerably less. Inhibition of acetylene-reduction activity by the addition of 32 mM orthophosphate was 14%, by 32 mM pyrophosphate 62%, by 0.2 atm of O2 65%, and by 0.5 atm of CO 12%; 0.5 atm of H2 had no effect. The molybdenum-glutathione complex also catalyzes the reduction of hydrazine to ammonia in a reaction that is dependent upon borohydride. The reaction is enhanced about 7-fold by ATP and proceeds at a rate of 2 mol of NH3 produced per min per mol of bound Mo.

Keywords: ATP requirement, nitrogenase comparison

Full text

PDF
339

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Burris R. H. Progress in the biochemistry of nitrogen fixation. Proc R Soc Lond B Biol Sci. 1969 Apr 1;172(1029):339–354. doi: 10.1098/rspb.1969.0025. [DOI] [PubMed] [Google Scholar]
  2. Dalton H., Morris J. A., Ward M. A., Mortenson L. E. Purification and some properties of molybdoferredoxin, a component of nitrogenase from Clostridium pasteurianum. Biochemistry. 1971 May 25;10(11):2066–2072. doi: 10.1021/bi00787a016. [DOI] [PubMed] [Google Scholar]
  3. Dalton H., Mortenson L. E. Dinitrogen (N 2 ) fixation (with a biochemical emphasis). Bacteriol Rev. 1972 Jun;36(2):231–260. doi: 10.1128/br.36.2.231-260.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Eady R. R., Smith B. E., Cook K. A., Postgate J. R. Nitrogenase of Klebsiella pneumoniae. Purification and properties of the component proteins. Biochem J. 1972 Jul;128(3):655–675. doi: 10.1042/bj1280655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hill R. E., Richards R. L. Reduction of dinitrogen in aqueous solution. Nature. 1971 Sep 10;233(5315):114–115. doi: 10.1038/233114a0. [DOI] [PubMed] [Google Scholar]
  6. Koch B., Evans H. J., Russell S. Reduction of acetylene and nitrogen gas by breis and cell-free extracts of soybean root nodules. Plant Physiol. 1967 Mar;42(3):466–468. doi: 10.1104/pp.42.3.466. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Schrauzer G. N., Doemeny P. A., Frazier R. H., Jr, Kiefer G. W. The chemical evolution of a nitrogenase model. V. The reduction of nitriles. J Am Chem Soc. 1972 Oct 18;94(21):7378–7385. doi: 10.1021/ja00776a019. [DOI] [PubMed] [Google Scholar]
  8. Shilov A., Denisov N., Efimov O., Shuvalov N., Shuvalova N., Shilova A. New nitrogenase model for reduction of molecular nitrogen in protonic media. Nature. 1971 Jun 18;231(5303):460–461. doi: 10.1038/231460a0. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES