Mutagenesis studies of the FeSII protein of Azotobacter vinelandii: Roles of histidine and lysine residues in the protection of nitrogenase from oxygen damage

Biochemistry

Volumn 38, Issue 17, 1999, Pages 5563-5571

  Lou, Jianrong ^a   Moshiri, Farhad ^a,b   Johnson, Michael K ^c   Lafferty, Meghan E ^c   Sorkin, David L ^a   Miller, A F ^a   Maier, Robert J ^a,c  

^a JOHNS HOPKINS UNIVERSITY   (United States)

^b MONSANTO COMPANY   (United States)

^c UNIVERSITY OF GEORGIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NITROGENASE; OXYGEN;

AMINO ACID SEQUENCE; ARTICLE; AZOTOBACTER VINELANDII; ENZYME ACTIVITY; ESCHERICHIA COLI; MUTAGENESIS; NITROGEN FIXATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION;

AZOTOBACTER VINELANDII; BACTERIAL PROTEINS; CARRIER PROTEINS; ENZYME ACTIVATION; ESCHERICHIA COLI; HISTIDINE; IRON-SULFUR PROTEINS; LYSINE; MUTAGENESIS, SITE-DIRECTED; NITROGENASE; OXYGEN; RECOMBINANT PROTEINS;

AZOTOBACTER; AZOTOBACTER VINELANDII; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033609129     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9827823     Document Type: Article

References (40)

1. Gallon, J. R. (1992) New Phytol. 122, 571-609.
2. Dean, D. R., and Jacobson, M. R. (1992) in Biological Nitrogen Fixation (Stacey, G., Burris, R. H., and Evans, H. J., Eds.) pp 763-834, Chapman and Hall, New York.
3. Kelly, M. J., Poole, R. K., Yates, M. G., and Kennedy, C. (1990) J. Bacteriol. 172, 6010-6019.
4. Shethna, Y. I., DerVartanian, D. V., and Beinert, H. (1968) Biochem. Biophys. Res. Commun. 31, 862-867.
5. Robson, R. L. (1979) Biochem. J. 181, 569-575.
6. Moshiri, F., Kim, J. W., Fu, C., and Maier, R. J. (1994) Mol. Microbiol. 14, 101-114.
7. Moshiri, F., Crouse, B. R., Johnson, M. K., and Maier, R. J. (1995) Biochemistry 34, 12973-12982.
8. Williams, A. M., and Wilson, P. W. (1954) J. Bacteriol. 67, 353-356.
9. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K. (1991) Current Protocols in Molecular Biology, Wiley-Interscience, New York.
10. Inubishi, T., and Becker, E. D. (1983) J. Magn. Reson. 51, 128-133.
11. Sorkin, D. L., and Miller, A.-F. (1997) Biochemistry 36, 4916-4924.
12. Wüthrich, K. (1986) NMR of Proteins and Nucleic Acids, Wiley, New York.
13. Waugh, S. I., Paulsen, D. M., Mylona, P. V., Maynard, R. H., Premakumar, R., and Bishop, P. E. (1995) J. Bacteriol. 177, 1505-1510.
14. Shah, V. K., Davis, L. C., and Brill, W. J. (1972) Biochim. Biophys. Acta 256, 498-511.
15. Dailey, H. A., Finnegan, M. G., and Johnson, M. K. (1994) Biochemistry 33, 403-407.
16. Fu, W., Drozdzewski, P. M., Davies, M. D., Sligar, S. G., and Johnson, M. K. (1992) J. Biol. Chem. 267, 15502-15510.
17. Ta, D. T., and Vickery, L. E. (1992) J. Biol. Chem. 267, 11120-11125.
18. Banci, L. Bertini, I., and Luchinat, C. (1990) Struct. Bonding (Berlin) 72, 113-118.
19. Oh, B. H., and Markley, J. L. (1990) Biochemistry 29, 4012-4017.
20. Skjeldahl, L., Markley, J. L., Coghlan, V. M., and Vickery, L. E. (1991) Biochemistry 30, 9078-9083.
21. Dugad, L. B., La Mar, G. N., Banci, L., and Bertini, I. (1990) Biochemistry 29, 2263-2271.
22. Jensen, G. M., Warshal, A., and Stephens, P. J. (1994) Biochemistry 33, 10911-10924.
23. Langen, R., Jensen, G. M., Jacob, U., Stephens, P. J., and Warshel, A. (1992) J. Biol. Chem. 267, 25625-25627.
24. Matsubara, H., and Saeki, K. (1992) in Iron-Sulfur Proteins (Cammack, R., Ed.) Advances in Inorganic Chemistry, Vol. 38, pp 223-280, Academic Press, San Diego, CA.
25. Scherings, G., Haaker, H., Wassink, H., and Veeger, C. (1983) Eur. J. Biochem. 135, 591-599.
26. Schmitz, S., Schrautemeier, B., and Bohme, H. (1993) Mol. Gen. Genet. 240, 455-461.
27. Veeger, C., Laane, C., Scherings, G., Matz, L., Haaker, H., and Van eeland-Wolbers, L. (1980) in Nitrogen Fixation (Newton, W. E., and Orme-Johnson, W. H., Eds.) Vol. 1, pp 111-137, University Park Press, Baltimore, MD.
28. Lambeth, J. D., Saybert, D. W., Lancaster, J. R., Jr., Salerno, J. C., and Kamin, H. (1982) Mol. Cell. Biochem. 45, 13-31.
29. Smith, E. T., Tomich, J. M., Iwamoto, T., Richards, J. H., Mao, Y., and Feinberg, B. A. (1991) Biochemistry 30, 11669-11676.
30. Haaker, H., and Veeger, C. (1977) Eur. J. Biochem. 77, 1-10.
31. Bulen, W. A., and LeComte, J. R. (1972) Methods Enzymol. 24, 456-470.
32. Wang, Z.-C., Burns, A., and Watt, G. D. (1985) Biochemistry 24, 214-221.
33. Bohme, H., and Haselkorn, R. (1988) Mol. Gen. Genet. 214, 278-285.
34. Masepohl, B., Scholisch, K., Gorlitz, K., Kutzki, C., and Bohme, H. (1997) Mol. Gen. Genet. 253, 770-776.
35. Miura, S., and Ichikawa, Y. (1991) Eur. J. Biochem. 197, 747-757.
36. Miura, S., Tomita, S., and Ichikawa, Y. (1991) J. Biol. Chem. 266, 19212-19216.
37. Xia, B., Cheng, H., Skjeldahl, L., Coghlan, V. M., Vickery, L. E., and Markley, J. L. (1995) Biochemistry 34, 180-187.
38. Cooper, D. Y., Schleyer, H., Levin, S. S., and Rosenthal, O. (1973) Ann. N.Y. Acad. Sci. 212, 227-247.
39. Salmeen, I., and Palmer, G. (1972) Arch. Biochem. Biophys. 150, 767-773.
40. Bishop, P. E., Jarlenski, D. M. L., and Hetherington, D. R. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 7342-7346.