Azotobacter vinelandii vanadium nitrogenase: Formaldehyde is a product of catalyzed HCN reduction, and excess ammonia arises directly from catalyzed azide reduction

Biochemistry

Volumn 45, Issue 13, 2006, Pages 4190-4198

  Fisher, Karl ^a   Dilworth, Michael J ^a,b   Newton, William E ^a  

^a VIRGINIA POLYTECHNIC INSTITUTE AND STATE UNIVERSITY   (United States)

^b MURDOCH UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; CATALYSIS; CYANIDES; HYDROLYSIS; MAGNETIC FLUX; NITROGEN COMPOUNDS; REDUCTION;

AZOTOBACTER VINELANDII VANADIUM NITROGENASE; CATALYZED AZIDE REDUCTION; MO-NITROGENASE; V-NITROGENASE;

ENZYMES;

ADENOSINE TRIPHOSPHATE MAGNESIUM; AMMONIA; AZIDE; CARBON MONOXIDE; CYANIDE; FORMALDEHYDE; METHANOL; MOLYBDENUM NITROGENASE; NITROGENASE; UNCLASSIFIED DRUG; VANADIUM; VANADIUM NITROGENASE;

ARTICLE; AZOTOBACTER VINELANDII; CATALYSIS; CELL GROWTH; ELECTRON TRANSPORT; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN PURIFICATION; REDUCTION;

AMMONIA; AZIDES; AZOTOBACTER VINELANDII; CARBON MONOXIDE; CATALYSIS; FORMALDEHYDE; HYDROGEN CYANIDE; NITROGENASE; OXIDATION-REDUCTION;

AZOTOBACTER VINELANDII;

EID: 33645550470     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0514109     Document Type: Article

References (50)

1. Luque, F., and Pau, R. N. (1991) Transcriptional regulation by metals of structural genes for Azotobacter vinelandii nitrogenases, Mol. Gen. Genet. 227, 481-487.
2. Newton, W. E. (1993) Nitrogenases: Distribution, composition, structure and function, in New Horizons in Nitrogen Fixation (Palacios, R., Mora, J., and Newton, W. E., Eds.) pp 5-18, Kluwer Academic, Dordrecht, The Netherlands.
3. Bortels, H. (1933) Short note on the catalysis of biological nitrogen fixation, Zentralbl. Bakteriol. Parasitenkd. 87, 476-477.
4. Bishop, P. E., Jarlenski, D. M. L., and Hetherington, D. R. (1980) Evidence for an alternative nitrogen fixation system in Azotobacter vinelandii, Proc. Natl. Acad. Sci. U.S.A. 77, 7342-7346.
5. Robson, R. L., Eady, R. R., Richardson, T. H., Miller, R. W., Hawkins, M. E., and Postgate, J. R. (1986) The alternative nitrogenase of Azotobacter chroococcum is a vanadium enzyme, Nature 322, 388-390.
6. Eady, R. R. (1996) Structure-function relationships of alternative nitrogenases, Chem. Rev. 96, 3013-3030.
7. Eady, R. R. (2003) Current status of structure function relationships of vanadium nitrogenase, Coord. Chem. Rev. 237, 23-30.
8. Smith, B. E., Eady, R. R., Lowe, D. J., and Gormal, C. (1988) The vanadium-iron protein of vanadium nitrogenase from Azotobacter chroococcum contains an iron-vanadium cofactor, Biochem. J. 250, 299-302.
9. Ravi, N., Moore, V., Lloyd, S. G., Hales, B. J., and Huynh, B. H. (1994) Mössbauer characterization of the metal clusters in Azotobacter vinelandii nitrogenase VFe protein, J. Biol. Chem. 269, 20920-20924.
10. 57Fe Mössbauer spectroscopy, J. Biol. Inorg. Chem. 7, 37-45.
11. Rees, D. C., and Howard, J. B. (2000) Nitrogenase: Standing at the crossroads, Curr. Opin. Chem. Biol. 4, 559-566.
12. Einsle, O., Tezcan, F. A., Andrade, S. L., Schmid, B., Yoshida, M., Howard, J. B., and Rees, D. C. (2002) Nitrogenase MoFe-protein at 1.16 Å resolution: A central ligand in the FeMo-cofactor, Science 297, 1696-1700.
13. Lowe, D. J., and Thorneley, R. N. F. (1984) The mechanism of Klebsiella pneumoniae nitrogenase action, Biochem. J. 224, 877-909.
14. Dilworth, M. J., and Eady, R. R. (1991) Hydrazine is a product of dinitrogen reduction by the vanadium-nitrogenase from Azotobacter chroococcum, Biochem. J. 277, 465-468.
15. Dilworth, M. J., Eady, R. R., and Eldridge, M. E. (1988) The vanadium nitrogenase of Azotobacter chroococcum, Biochem. J. 249, 745-751.
16. Maskos, Z., and Hales, B. J. (2002) Photo-lability of CO bound to Mo-nitrogenase from Azotobacter vinelandii, J. Inorg. Biochem. 93, 11-17.
17. Biggins, D. R., and Kelly, M. (1970) Interaction of nitrogenase from Klebsiella pneumoniae with ATP or cyanide, Biochim. Biophys. Acta 205, 288-299.
18. 2-fixing enzymes of Azotobacter vinelandii and Clostridium pasteurianum, Biochim. Biophys. Acta 139, 69-90.
19. Li, J. G., Burgess, B. K., and Corbin, J. L. (1982) Nitrogenase reactivity: Cyanide as substrate and inhibitor, Biochemistry 21, 4393-4402.
20. -, Biochemistry 39, 10855-10865.
21. Wilson, C. L., and Wilson D. W. (1962) Comprehensive Analytical Chemistry, p 289, Elsevier, London.
22. von Richter, V. (1947) in Richter's Organic Chemistry (Anschütz, R., and Reindel, F., Eds.) 3rd ed. (English), Vol. 1, p 245, Elsevier, London.
23. Nash, T. (1953) The colorimetric estimation of formaldehyde by means of the Hantzsch reaction, Biochem. J. 55, 416-421.
24. Dilworth, M. J., and Thorneley, R. N. F. (1981) Nitrogenase of Klebsiella pneumoniae: Hydrazine is as product of azide reduction, Biochem. J. 193, 971-983.
25. Rubinson, J. F., Burgess, B. K., Corbin, J. L., and Dilworth, M. J. (1985) Nitrogenase reactivity: Azide reduction, Biochemistry 24, 273-283.
26. Gln- substituted MoFe proteins of Azotobacter vinelandii nitrogenase, Biochemistry 39, 15570-15577.
27. Joerger, R. D., Wolfinger, E. D., and Bishop, P. E. (1991) The gene encoding dinitrogenase reductase-2 is required for expression of the second alternative nitrogenase from Azotobacter vinelandii, J. Bacteriol. 173, 4440-4446.
28. Premakumar, R., Loveless, T. M., and Bishop, P. E. (1994) Effect of amino acid substitutions in a potential metal-binding site of AnfA on expression from the anfH promoter in Azotobacter vinelandii, J. Bacteriol. 176, 6139-6142.
29. Kim, C. H., Newton, W. E., and Dean, D. R. (1995) Role of the MoFe protein α-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis, Biochemistry 34, 2798-2808.
30. Blanchard, C. Z., and Hales, B. J. (1996) Isolation of two forms of the nitrogenase VFe protein from Azotobacter vinelandii, Biochemistry 35, 472-478.
31. Ennor, A. H. (1957) Determination and preparation of N-phosphates of biological origin, Methods Enzymol. 3, 850-856.
32. 3 in steady-state nitrogenase assays, Anal. Biochem. 207, 6-10.
33. Fawcett, J. K., and Scott, J. E. (1960) Determination of ammonia using indophenol, J. Clin. Pathol. 13, 156-159.
34. 3 produced during nitrogenase assays, Anal. Biochem. 256, 242-244.
35. Herzberg, G. R., and Rogerson, M. (1985) Use of alcohol oxidase to measure the methanol produced during the hydrolysis of D- and L-methyl-3-hydroxybutyric acid, Anal. Biochem. 149, 354-357.
36. Benton, P. M., Laryukhin, M., Mayer, S. M., Hoffman, B. M., Dean, D. R., and Seefeldt, L. C. (2003) Localization of a substrate binding site on the FeMo-cofactor in nitrogenase: Trapping propargyl alcohol with an α-70-substituted MoFe protein, Biochemistry 42, 9102-9109.
37. Igarashi, R. Y., Dos Santos, P. C., Niehaus, W. G., Dance, I. G., Dean, D. R., and Seefeldt, L. C. (2004) Localization of a catalytic intermediate bound to the FeMo-cofactor of nitrogenase, J. Biol. Chem. 279, 34770-34775.
38. Lee, H. I., Igarashi, R. Y., Laryukhin, M., Doan, P. E., Dos Santos, P. C., Dean, D. R., Seefeldt, L. C., and Hoffman, B. M. (2004) An organometallic intermediate during alkyne reduction by nitrogenase, J. Am. Chem. Soc. 126, 9563-9569.
39. Davis, L. C., Henzl, M. T., Burris, R. H., and Orme-Johnson, W. H. (1979) Iron-sulfur clusters in the molybdenum-iron protein component of nitrogenase. Electron paramagnetic resonance of the carbon monoxide inhibited state, Biochemistry 18, 4860-4869.
40. Shen, J., Dean, D. R., and Newton, W. E. (1997) Evidence for multiple substrate-reduction sites and distinct inhibitor-binding sites from an altered Azotobacter vinelandii nitrogenase MoFe protein, Biochemistry 36, 4884-4894.
41. Christiansen, J., Seefeldt, L. C., and Dean, D. R. (2000) Competitive substrate and inhibitor interactions at the physiologically relevant active site of nitrogenase, J. Biol. Chem. 275, 36104-36107.
42. 2 reduction, Biochemistry 43, 2947-2956.
43. Burns, A., Watt, G. D., and Wang, Z. C. (1985) Salt inhibition of nitrogenase catalysis and salt effects on the separate protein components, Biochemistry 24, 3932-3936.
44. Deits, T. L., and Howard, J. B. (1990) Effects of salts on Azotobacter vinelandii nitrogenase activities, J. Biol. Chem. 265, 3859-3867.
45. Lowe, D. J., Fisher, K., Thorneley, R. N. F., Vaughn, S. A., and Burgess, B. K. (1989) Kinetics and mechanism of the reaction of cyanide with molybdenum nitrogenase from Azotobacter vinelandii, Biochemistry 28, 8460-8466.
46. Maskos, Z., Fisher, K., Sørlie, M., Newton, W. E., and Hales, B. J. (2005) Variant MoFe proteins of Azotobacter viinelandii: Effects of carbon monoxide on electron paramagnetic resonance spectra generated during enzyme turnover, J. Biol. Inorg. Chem. 10, 394-406.
47. Dilworth, M. J., Fisher, K., Kim, C. H., and Newton, W. E. (1998) Effects on substrate reduction of substitution of histidine-195 by glutamine in the α-subunit of the Azotobacter vinelandii MoFe protein of Azotobacter vinelandii nitrogenase, Biochemistry 37, 17495-17505.
48. 2 reduction by V nitrogenase from Azotobacter vinelandii, J. Am. Chem. Soc. 118, 279-280.
49. Cameron, L. M., and Hales, B. J. (1998) Investigation of CO binding and release from Mo-nitrogenase during catalytic turnover, Biochemistry 37, 9449-9456.
50. Moore, V. G., Tittsworth, R. C., and Hales, B. J. (1994) Construction and characterization of hybrid component I from V-nitrogenase containing FeMo-cofactor, J. Am. Chem. Soc. 116, 12101-12102.