Abstract

The nitrogenase system consists of two components, an iron (Fe-) protein and a molybdenum-iron (MoFe-) protein, which reduce dinitrogen in an ATP dependent reaction. The fundamental role of ATP and the Fe-protein in the mechanism of nitrogenase will be examined by X-ray diffraction studies of recently crystallized Fe-protein from Azotobacter vinelandii. The main areas to be investigated are: 1) the nature and environment of metal centers in Fe-protein; 2) the molecular symmetry of Fe-protein; 3) location of the ATP binding site, and the possible structural consequences of ATP binding; 4) distribution of conserved and nonconserved residues in the three-dimensional structure, and the implications for Fe-protein function. The Fe-protein structure will provide a framework for correlating an extensive body of spectroscopic, kinetic and chemical studies on the nitrogenase system.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM031875-03
Application #
3280288
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1983-04-01
Project End
1986-03-31
Budget Start
1985-04-01
Budget End
1986-03-31
Support Year
3
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of California Los Angeles
Department
Type
Schools of Arts and Sciences
DUNS #
119132785
City
Los Angeles
State
CA
Country
United States
Zip Code
90095

  Publications

Allen, J P; Feher, G; Yeates, T O et al. (1988) Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions. Proc Natl Acad Sci U S A 85:8487-91
Komiya, H; Yeates, T O; Rees, D C et al. (1988) Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species. Proc Natl Acad Sci U S A 85:9012-6
Yeates, T O; Komiya, H; Chirino, A et al. (1988) Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions. Proc Natl Acad Sci U S A 85:7993-7
Yeates, T O; Komiya, H; Rees, D C et al. (1987) Structure of the reaction center from Rhodobacter sphaeroides R-26: membrane-protein interactions. Proc Natl Acad Sci U S A 84:6438-42
Chakrabarti, P; Bernard, M; Rees, D C (1986) Peptide-bond distortions and the curvature of alpha-helices. Biopolymers 25:1087-93
Allen, J P; Feher, G; Yeates, T O et al. (1986) Structural homology of reaction centers from Rhodopseudomonas sphaeroides and Rhodopseudomonas viridis as determined by x-ray diffraction. Proc Natl Acad Sci U S A 83:8589-93
Dickerson, J L; Kornuc, J J; Rees, D C (1985) Complex formation between flavodoxin and cytochrome c. Cross-linking studies. J Biol Chem 260:5175-8
Rees, D C (1985) Electrostatic influence on energetics of electron transfer reactions. Proc Natl Acad Sci U S A 82:3082-5
Lewis, M; Rees, D C (1985) Fractal surfaces of proteins. Science 230:1163-5