Trapping an intermediate of dinitrogen (N2) reduction on nitrogenase

Biochemistry

Volumn 48, Issue 38, 2009, Pages 9094-9102

  Barney, Brett M ^a   Lukoyanov, Dmitriy ^c   Igarashi, Robert Y ^a,d   Laryukhin, Mikhail ^a,c   Yang, Tran Chin ^c   Dean, Dennis R ^b   Hoffman, Brian M ^c   Seefeldt, Lance C ^a  

^a UTAH STATE UNIVERSITY   (United States)

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

^c NORTHWESTERN UNIVERSITY   (United States)

^d UNIVERSITY OF CENTRAL FLORIDA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SUBSTITUTION; AMMONIA MOLECULES; COFACTORS; DERIVED SPECIES; DIAZENES; DINITROGEN; ELECTRON FLUX; EPR SIGNALS; FE-PROTEINS; FIELD DEPENDENCE; HIGH CONCENTRATION; HYPERFINE TENSORS; INTERMEDIATE STATE; LINEAR DEPENDENCE; MICROWAVE POWER; NON-LINEAR RESPONSE; NUCLEAR SPINS; PH OPTIMA; REDUCTION OF PROTONS; RESTING STATE; SIGNAL INTENSITIES; SQUARE ROOTS; WILD TYPES;

ACETYLENE; AMINES; AMINO ACIDS; ELECTRON RESONANCE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ORGANIC ACIDS; PARAMAGNETIC RESONANCE; PROTONS; QUANTUM THEORY; SPECTROSCOPIC ANALYSIS; SPIN DYNAMICS;

SUBSTRATES;

AMMONIA; DIAMIDE; DINITROGEN; DINITROGENASE REDUCTASE; HYDRAZINE; HYDROGEN; METHYLDIAZENE; MOLYBDENUM IRON PROTEIN; NITROGEN; NITROGEN 15; NITROGENASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; AZOTOBACTER VINELANDII; CONCENTRATION RESPONSE; ELECTRON NUCLEAR DOUBLE RESONANCE; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; MICROWAVE IRRADIATION; NITROGEN DEPOSITION; NITROGEN DYNAMICS; NITROGEN UTILIZATION; NONHUMAN; PH MEASUREMENT; PRIORITY JOURNAL; PROCESS OPTIMIZATION; PROTON TRANSPORT; STEADY STATE; CHEMISTRY; ENZYME STABILITY; ENZYMOLOGY; FREEZING; METABOLISM; OXIDATION REDUCTION REACTION; PH;

AZOTOBACTER VINELANDII; BACTERIAL PROTEINS; CATALYTIC DOMAIN; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT; ENZYME STABILITY; FREEZING; HYDROGEN-ION CONCENTRATION; MOLYBDOFERREDOXIN; NITROGEN; OXIDATION-REDUCTION;

EID: 70349785252     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901092z     Document Type: Article

References (37)

1. Burgess, B. K., and Lowe, D. J. (1996) The mechanism of molybdenum nitrogenase. Chem. Rev. 96, 2983-3011.
2. Seefeldt, L. C., Hoffman, B. M., and Dean, D. R. (2009) Mechanism of Mo-dependent nitrogenase. Annu. Rev. Biochem. 78, 701-722.
3. Hoffman, B. M., Dean, D. R., and Seefeldt, L. C. (2009) Climbing nitrogenase: Toward a mechanism of enzymatic nitrogen fixation. Acc. Chem. Res. 42, 609-619.
4. Rees, D. C., Tezcan, F. A., Haynes, C. A., Walton, M. Y., Andrade, S., Einsle, O., and Howard, J. B. (2005) Structural basis of biological nitrogen fixation. Philos. Trans. R. Soc. London, Ser. A 363, 971-984.
5. Shah, V. K., and Brill, W. J. (1977) Isolation of an iron-molybdenum cofactor from nitrogenase. Proc. Natl. Acad. Sci. U.S.A. 74, 3249-3253.
6. Howard, J. B., and Rees, D. C. (1996) Structural basis of biological nitrogen fixation. Chem. Rev. 96, 2965-2982.
7. Einsle, O., Tezcan, F. A., Andrade, S. L. A., Schmid, B., Yoshida, M., Howard, J. B., and Rees, D. C. (2002) Nitrogenase MoFe-protein at 1.16 angstrom resolution: A central ligand in the FeMo-cofactor. Science 297, 1696-1700. (Pubitemid 35000783)
8. Hageman, R. V., and Burris, R. H. (1978) Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle. Proc. Natl. Acad. Sci. U.S.A. 75, 2699-2702.
9. Burgess, B. K. (1985) Substrate reactions of nitrogenase. In Metal Ions in Biology: Molybdenum Enzymes (Spiro, T. G., Ed.) pp 161-220, John Wiley and Sons, New York.
10. Simpson, F. B., and Burris, R. H. (1984)Anitrogen pressure of 50 atm does not prevent evolution of hydrogen by nitrogenase. Science 224, 1095-1097.
11. Kim, J., and Rees, D. C. (1992) Crystallographic structure and functional implications of the nitrogenase molybdenum iron protein from Azotobacter vinelandii. Nature 360, 553-560. (Pubitemid 23000704)
12. Kim, J., and Rees, D. C. (1992) Structural models for the metal centers in the nitrogenase molybdenum-iron protein. Science 257, 1677-1682.
13. Chan, M. K., Kim, J., and Rees, D. C. (1993) The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 Å resolution structures. Science 260, 792-794. (Pubitemid 23167606)
14. Christiansen, J., Cash, V. L., Seefeldt, L. C., and Dean, D. R. (2000) Isolation and characterization of an acetylene-resistant nitrogenase. J. Biol. Chem. 275, 11459-11464.
15. 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.
16. Mayer, S. M., Niehaus, W. G., and Dean, D. R. (2002) Reduction of short chain alkynes by a nitrogenase α-70Ala-substituted MoFe protein. J. Chem. Soc., Dalton Trans. 5, 802-807. (Pubitemid 35206647)
17. 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.
18. 2 and CO. J. Am. Chem. Soc. 127, 15880-15890.
19. - bound to the nitrogenase FeMo-cofactor active site during H2 evolution: Characterization by ENDOR spectroscopy. J. Am. Chem. Soc. 127, 6231-6241.
20. 2 binding state. Proc. Natl. Acad. Sci. U.S.A. 104, 1451-1455.
21. Thorneley, R.N. F., and Lowe, D. J. (1985) Kinetics and mechanisms of the nitrogenase enzyme system. In Molybdenum Enzymes (Spiro, T. G., Ed.) pp 221-284, John Wiley and Sons, New York.
22. 2. J. Am. Chem. Soc. 127, 14960-14961.
23. Christiansen, J., Goodwin, P. J., Lanzilotta, W. N., Seefeldt, L. C., and Dean, D. R. (1998) Catalytic and biophysical properties of a nitrogenase apo-MoFe protein produced by a nifB-deletion mutant of Azotobacter vinelandii. Biochemistry 37, 12611-12623. (Pubitemid 28427546)
24. Barney, B. M., Laryukhin, M., Igarashi, R. Y., Lee, H. I., Dos Santos, P. C., Yang, T. C., Hoffman, B. M., Dean, D. R., and Seefeldt, L. C. (2005) Trapping a hydrazine reduction intermediate on the nitrogenase active site. Biochemistry 44, 8030-8037. (Pubitemid 40776664)
25. Hoffman, B. M., DeRose, V. J., Doan, P. E., Gurbiel, R. J., Houseman, A. L. P., and Telser, J. (1993) Metalloenzyme active-site structure and function through multifrequency CW and pulsed ENDOR. In Biological Magnetic Resonance (Berliner, L. J., and Reuben, J., Eds.) pp 151-218, Plenum Press, New York.
26. Davis, L. C., and Orme-Johnson, W. H. (1976) Nitrogenase IX: Effects of the MgATP generator on the catalytic and EPR properties of the enzyme in vitro. Biochim. Biophys. Acta 452, 42-58.
27. Rivera-Ortiz, J. M., and Burris, R. H. (1975) Interactions among substrates and inhibitors of nitrogenase. J. Bacteriol. 123, 537-545.
28. Barney, B. M., Igarashi, R. Y., Dos Santos, P. C., Dean, D. R., and Seefeldt, L.C. (2004) Substrate interaction at an iron-sulfur face of the FeMo-cofactor during nitrogenase catalysis. J. Biol. Chem. 279, 53621-53624.
29. Fisher, K., Newton, W. E., and Lowe, D. J. (2001) Electron paramagnetic resonance analysis of different Azotobacter vinelandii nitrogenase MoFe-protein conformations generated during enzyme turnover: Evidence for S=3/2 spin states from reduced MoFeprotein intermediates. Biochemistry 40, 3333-3339. (Pubitemid 32221635)
30. Burgess, B. K., Wherland, S., Newton, W. E., and Stiefel, E. I. (1981) Nitrogenase reactivity: Insight into the nitrogen-fixing process through hydrogen-inhibition and HD-forming reactions. Biochemistry 20, 5140-5146.
31. 3) derived species bound to the nitrogenase active site FeMo-cofactor: Implications for mechanism. Proc. Natl. Acad. Sci. U.S.A. 103, 17113-17118.
32. 2 reduction. Biochemistry 46, 6784-6794.
33. Lee, H. I., Benton, P. M., Laryukhin, M., Igarashi, R. Y., Dean, D. R., Seefeldt, L. C., and Hoffman, B.M. (2003) The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM show it is not an exchangeable nitrogen. J. Am. Chem. Soc. 125, 5604-5605.
34. Benton, P. M. C., Laryukhin, M., Mayer, S. M., Hoffman, B. M., Dean, D. R., and Seefeldt, L. C. (2003) Localization of a substrate binding site on FeMo-cofactor in nitrogenase: Trapping propargyl alcohol with an α-70-substituted MoFe protein. Biochemistry 42, 9102-9109. (Pubitemid 36935418)
35. Kim, C. H., Newton, W. E., and Dean, D. R. (1995) Role of the MoFe protein R-subunit histidine-195 residue in FeMo-cofactor binding and nitrogenase catalysis. Biochemistry 34, 2798-2808.
36. Lukoyanov, D., Pelmenschikov, V., Maeser, N., Laryukhin, M., Yang, T. C., Noodleman, L., Dean, D. R., Case, D. A., Seefeldt, L. C., and Hoffman, B. M. (2007) Testing if the interstitial atom, X, of the nitrogenase molybdenum-iron cofactor is N or C: ENDOR, ESEEM, and DFT studies of the S = 3/2 resting state in multiple environments. Inorg. Chem. 46, 11437-11449.
37. DeRose, V. J., Liu, K. E., Lippard, S. J., and Hoffman, B. M. (1996) Investigation of the dinuclear Fe center of methane monooxygenase by advanced paramagnetic resonance techniques: On the geometry of DMSO binding. J. Am. Chem. Soc. 118, 121-134.