Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM033965-09A4
Application #
2177215
Study Section
Metallobiochemistry Study Section (BMT)
Project Start
1985-09-05
Project End
1998-05-31
Budget Start
1996-06-01
Budget End
1997-05-31
Support Year
9
Fiscal Year
1996
Total Cost
Indirect Cost

  Institution

Name
Louisiana State University A&M Col Baton Rouge
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
075050765
City
Baton Rouge
State
LA
Country
United States
Zip Code
70803

  Publications

Ravi, N; Moore, V; Lloyd, S G et al. (1994) Mossbauer characterization of the metal clusters in Azotobacter vinelandii nitrogenase VFe protein. J Biol Chem 269:20920-4
Onate, Y A; Finnegan, M G; Hales, B J et al. (1993) Variable temperature magnetic circular dichroism studies of reduced nitrogenase iron proteins and [4Fe-4S]+ synthetic analog clusters. Biochim Biophys Acta 1164:113-23
Oliver, M E; Hales, B J (1993) Using dysprosium complexes to probe the nitrogenase paramagnetic centers. Biochemistry 32:6058-64
Hales, B J; Case, E E (1987) Nitrogen fixation by Azotobacter vinelandii in tungsten-containing medium. J Biol Chem 262:16205-11
Morningstar, J E; Johnson, M K; Case, E E et al. (1987) Characterization of the metal clusters in the nitrogenase molybdenum-iron and vanadium-iron proteins of Azotobacter vinelandii using magnetic circular dichroism spectroscopy. Biochemistry 26:1795-800
Hales, B J; Case, E E; Morningstar, J E et al. (1986) Isolation of a new vanadium-containing nitrogenase from Azotobacter vinelandii. Biochemistry 25:7251-5
Hales, B J; Langosch, D J; Case, E E (1986) Isolation and characterization of a second nitrogenase Fe-protein from Azotobacter vinelandii. J Biol Chem 261:15301-6