The aims of this proposal are to: (1) identify the exposed and chemically susceptible amino acid residues on the PSII polypeptides after various treatments to selectively remove extrinsic proteins and heterogeneous Mn clusters, (2) identify protein domains capable of being x-linked, (3) characterize the structure of a possible extrinsic domain hetero-trimer complex, and (4) use vibrational spectroscopy and circular dichroism to predict the overall secondary structure of each extrinsic protein. %%% Water oxidation (oxygen evolution) during photosynthesis is one of the key reactions for all the living creatures on this planet. The studies proposed will characterize the interactions among the proteins involved in oxygen evolution in spinach. In contributing to an understanding of protein-protein and protein-metal ion interactions in living systems these studies may lead to the discovery of approaches to the formation of synthetic complexes capable of multielectron catalysis on large scales.

Agency
National Science Foundation (NSF)
Institute
Division of Molecular and Cellular Biosciences (MCB)
Application #
9304955
Program Officer
Marcia Steinberg
Project Start
Project End
Budget Start
1993-09-01
Budget End
1997-08-31
Support Year
Fiscal Year
1993
Total Cost
$319,000
Indirect Cost
Name
Louisiana State University & Agricultural and Mechanical College
Department
Type
DUNS #
City
Baton Rouge
State
LA
Country
United States
Zip Code
70803