1 |
Stephens, P. J., McKenna, C. E., Smith, B. E., Nguyen, H. T., McKenna, M. C., Thomson, A. J., Devlin, F., and Jones, J. B. 1979. Circular dichroism and magnetic circular dichroism of nitrogenase proteins. Proc. Natl. Acad. Sci. U.S.A. 76, 2585-2589
DOI
ScienceOn
|
2 |
Walker, G. A., and Mortenson, L. E. 1974. Effect of magnesium adenosine 5'-triphosphate on the accessibility of the iron of clostridial azoferredoxin, a component of nitrogenase. Biochemistry 13, 2382-2388
DOI
ScienceOn
|
3 |
Watt, G. D., Wang, Z. C., and Knotts, R. R. 1986. Redox reactions of and nucleotide binding to the iron protein of Azotobacter vinelandii. Biochemistry 25, 8156-8162
DOI
|
4 |
Wolle, D., Dean, D. R., and Howard, J. B. 1992. Nucleotide- iron-sulfur cluster signal transduction in the nitrogenase iron-protein: the role of Asp125. Science 258, 992-995
DOI
|
5 |
Zumft, W. G., Palmer, G., and Mortenson, L. E. 1973. Electron paramagnetic resonance studies on nitrogenase. II. Interaction of adenosine 5'-triphosphate with azoferredoxin. Biochim. Biophys. Acta. 292, 413-421
DOI
ScienceOn
|
6 |
Ryle, M. J. and Seefeldt, L. C. 1996. Elucidation of a MgATP signal transduction pathway in the nitrogenase iron protein: formation of a conformation resembling the MgATP-bound state by protein engineering. Biochemistry 35, 4766-4775
DOI
ScienceOn
|
7 |
Ryle, M. J., Lanzilotta, W. N., and Seefeldt, L. C. 1996. Elucidating the mechanism of nucleotide-dependent changes in the redox potential of the [4Fe-4S] cluster in nitrogenase iron protein: the role of phenylalanine 135.Biochemistry 35, 9424-9434
DOI
ScienceOn
|
8 |
Simpson, F. B. and Burris, R. H. 1984. A nitrogen pressure of 50 atmospheres does not prevent evolution of hydrogen by nitrogenase. Science 224, 1095-1097
DOI
|
9 |
Schindelin, H., Kisker, C., Schtessman, J. L., Howard, J. B., and Rees, D. C. 1997. Structure of ADP AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature 387, 370-376
DOI
ScienceOn
|
10 |
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
DOI
ScienceOn
|
11 |
Smith, B. E. and Eady, R. R. 1992. Metalloclusters of the nitrogenases. Eur. J. Biochem. 205, 1-15
DOI
ScienceOn
|
12 |
Spee, J. H., Arendsen, A. F., Wassink, H., Marritt, S. J., Hagen, W. R., and Haaker, H. 1998. Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase. FEBS Lett. 432, 55-58
DOI
ScienceOn
|
13 |
Stephens, P. J., Jollie, D. R., and Warshel, A. 1996. Protein control of redox potentials of ironminus sign sulfur proteins. Chem. Rev. 96, 2491-2513
DOI
ScienceOn
|
14 |
Lindahl, P. A., Gorelick, N. J., Mnck, E., and Orme-Johnson, W. H. 1987. EPR and Mossbauer studies of nucleotide-bound nitrogenase iron protein from Azotobacter vinelandii. J. Biol. Chem. 262, 14945-14953
|
15 |
Mortenson, L. E., Seefeldt, L. C., Morgan, T. V. and Bolin, J. T. 1993. The role of metal clusters and MgATP in nitrogenase catalysis. Adv. Enzymol. Rel. Areas Mol. Biol. 67, 274-299
|
16 |
Peters, J. W., Fisher, K., and Dean, D. R. 1995. Nitrogenase structure and function: A biochemical-genetic perspective. Annu. Rev. Microbiol. 49, 335-366
DOI
ScienceOn
|
17 |
Ljones, T. and Burris, R. H. 1978. Nitrogenase: the reaction between the Fe protein and bathophenanthrolinedisulfonate as a probe for interactions with MgATP. Biochemistry 17, 1866-1872
DOI
|
18 |
Meyer, J., Gaillard, J., and Moulis, J. M. 1988. Hydrogen-1 nuclear magnetic resonance of the nitrogenase iron protein (Cp2) from Clostridium pasteurianum. Biochemistry 27, 6150-6156
DOI
ScienceOn
|
19 |
Nicholls, A., Sharp, K. A., and Honig, B. 1991. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons Proteins 11, 281-296
DOI
ScienceOn
|
20 |
Renner, K. A., and Howard, J. B. 1996. Aluminum fluoride inhibition of nitrogenase: stabilization of a nucleotide.Fe- protein.MoFe-protein complex. Biochemistry 35, 5353-5358.
DOI
ScienceOn
|
21 |
Ryle, M. J., Lanzilotta, W. N., Seefeldt, L. C., Scarrow, R. C., and Jensen, G. M. 1996. Circular dichroism and x-ray spectroscopies of Azotobacter vinelandii nitrogenase iron protein. MgATP and MgADP induced protein conformational changes affecting the [4Fe-4S] cluster and characterization of a [2Fe-2S] form. J. Biol. Chem. 271, 1551- 1557
DOI
|
22 |
Jang, S. B., Seefeldt, L. C., and Peters, J. W. 2000. Modulating the midpoint potential of the [4Fe-4S] cluster of the nitrogenase Fe protein. Biochemistry 39, 641-648
DOI
ScienceOn
|
23 |
Lanzilotta, W. N., Holz, R. C., and Seefeldt, L. C. 1995. Proton NMR investigation of the [4Fe-4S]1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes. Biochemistry 34, 15646-15653
DOI
ScienceOn
|
24 |
Jensen, G. M., Warshel, A., and Stephens, P. J. 1994. Calculation of the redox potentials of iron-sulfur proteins: the 2-/3-couple of [Fe4S*4Cys4] clusters in Peptococcus aerogenes ferredoxin, Azotobacter vinelandii ferredoxin I, and Chromatium vinosum high-potential iron protein. Biochemistry 33, 10911-10924
DOI
|
25 |
Langen, R., Jensen, G. M., Jacob, U., Stephens, P. J., and Warshel, A. 1992. Protein control of iron-sulfur cluster redox potentials. J. Biol. Chem. 267, 25625-25627
|
26 |
Lanzilotta, W. N., and Seefeldt, L. C. 1997. Changes in the midpoint potentials of the nitrogenase metal centers as a result of iron protein-molybdenum-iron protein complex formation. Biochemistry 36, 12976-12983
DOI
ScienceOn
|
27 |
Lanzilotta, W. N., Fisher, K., and Seefeldt, L. C. 1997. Evidence for electron transfer-dependent formation of a nitrogenase iron protein-molybdenum-iron protein tight complex. The role of aspartate 39.J. Biol. Chem. 272, 4157-65
DOI
ScienceOn
|
28 |
Lanzilotta, W. N., Ryle, M. J., and Seefeldt, L. C. 1995. Nucleotide hydrolysis and protein conformational changes in Azotobacter vinelandii nitrogenase iron protein: defining the function of aspartate 129. Biochemistry 34, 10713-10723
DOI
ScienceOn
|
29 |
Georgiadis, M. M., Komiya, H., Chakrabarti, P., Woo, D., Kornuc, J. J., and Rees, D. C. 1992. Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257, 1653-1659
DOI
|
30 |
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
DOI
ScienceOn
|
31 |
Heering, H. A., Bulsink, Y. B. M., Hagen, W. R., and Meyer, T. E. 1995. Reversible super-reduction of the cubane [4Fe-4S](3+;2+;1+) in the high-potential iron-sulfur protein under non-denaturing conditions. EPR spectroscopic and electrochemical studies. Eur. J. Biochem. 232, 811-817
DOI
|
32 |
Howard, J. B. and Rees, D. C. 1994. Nitrogenase: a nucleotide-dependent molecular switch. Annu. Rev. Biochem. 63, 235-264
DOI
ScienceOn
|
33 |
Howard, J. B., and Rees, D. C. 1996. Structural Basis of Biological Nitrogen Fixation. Chem. Rev. 96, 2965-2982
DOI
ScienceOn
|
34 |
Jacobson, M. R.; Brigle, K. E.; Bennett, L. T., Setterquist, R. A.; Wilson, M. S., Cash, V. L., Beyon, J., Newton, W. E., Dean, D. R. 1989. Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii. J. Bacteriol. 171, 1017-1027
|
35 |
Jang, S. B., Seefeldt, L. C., and Peters, J. W. 2000. Insights into nucleotide signal transduction in nitrogenase: structure of an iron protein with MgADP bound. Biochemistry 39, 14745-14752
DOI
ScienceOn
|
36 |
Jang, S. B., Jeong, M. S., Seefeldt, L. C., Peters, J. W. 2004. Physical and genetic map of the major nif gene cluster from Azotobacter vinelandii. accepted to J. Biol. Inorg. Chem
|
37 |
Breiter, D. R., Meyer, T. E., Rayment, L., and Holden, H. M. 1991. The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution. J. Biol. Chem. 266, 18660-18667
|
38 |
Burgess, B. K. and Lowe, D. J. 1996. Mechanism of molybdenum nitrogenase. Chem. Rev. 96, 2983-3011
DOI
ScienceOn
|
39 |
Brigle, K. E.; Newton, W. E.; Dean, D. R. 1985. Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase structural gene cluster. Gene 37, 37-44
DOI
ScienceOn
|
40 |
Burgess, B. K. 1984. In advances in nitrogen fixation. pp. 103-114, In Veeger, C. and Newton, W. E. (eds.), Martinus Nijhoff, Boston
|
41 |
Burris, R. H. (1991) Nitrogenases. J. Biol. Chem. 266, 9339-9342
|
42 |
Carter, C. W., Jr., Kraut, J., Freer, S. T., Xuong, N. H., Alden, R. A., and Bartsch, R. G. 1974. Two-Angstrom crystal structure of oxidized Chromatium high potential iron protein. J. Biol. Chem. 249, 4212-4225
|
43 |
Chen, L., Gavini, N., Tsuruta, H., Eliezer, D., Burgess, B. K., Doniach, S., and Hodgson, K. O. 1994. MgATP-induced conformational changes in the iron protein from Azotobacter vinelandii, as studied by small-angle x-ray scattering. J. Biol. Chem. 269, 3290-3294
|
44 |
Duyvis, M. G., Wassink, H., and Haaker, H. 1996. Formation and characterization of a transition state complex of Azotobacter vinelandii nitrogenase. FEBS Lett. 380, 233-236
DOI
ScienceOn
|
45 |
Esnouf, R. M. 1997. An extensively modified version of MolScript that includes greatly enhanced coloring capabilities. J. Mol. Graph Model. 15, 132-134
DOI
ScienceOn
|
46 |
Adman, E., Watenpaugh, K. D., and Jensen, L. H. 1975. NH---S hydrogen bonds in Peptococcus aerogenes ferredoxin, Clostridium pasteurianum rubredoxin, and Chromatium high potential iron protein. Proc. Natl. Acad. Sci. USA 72, 4854-4858
DOI
ScienceOn
|