Collaborative Research:  Site-Directed Mutagenesis of the   Manganese Stabilizing Protein of Photosynthesis
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Kamal Shukla', 'PO_EMAI': None, 'PO_PHON': None}
The molecular events leading to photosynthetic water                            oxidation are still largely unknown, particularly the                           proteins involved and the specific residues that form ligands                   to manganese, an essential cofactor for oxygen evolution.                       Current models suggest the participation of the reaction                        center D1D2 complex and an extrinsic 33kD protein, called the                   manganese stabilizing protein.  This research will combine                      the techniques of site-directed mutagenesis, using the                          readily transformable cyanobacterium Synechocystis 6803, to                     modify selected amino acid residues comprising the so-called                    manganese stabilizing polypeptide, together with EPR and                        ENDOR spectroscopic methods which enable a direct assessment                    of these changes on the structure and kinetic properties of                     the manganese site and other endogenous electron donors                         coupled to the reaction center, such as Cytb559 and Tyr-                        160.%%%                                                                                                                                                         Photosynthesis is the most pervasive biological reaction on                     the face of the earth.  It produces nearly all of the oxygen                    in the air which is essential for oxidative metabolism in all                   aerobic organisms and for combustion in fossil fuel powered                     engines.  Thus, photosynthetic O2 evolution powers most                         biological and commercial machines.  Presently there are no                     man-made catalysts capable of carrying out the efficient                        evolution of O2 from water and an energy source with a                          commercially useful yield.  Nature, on the other hand, has                      developed a unique enzyme, found in all O2-evolving plants                      and algae, optimized for catalyzing this process.  This                         research will contribute to the understanding of the                            molecular basis by which green plants are capable of                            harnessing nature's most power oxidant, the splitting of the                    water by a manganese-containing enzyme.  By understanding                       this biological process we hope to gain insight that will                       lead to a new blueprint for the design of synthetic water                       oxidizing catalysts.***  //
{'FirstName': 'Barbara', 'LastName': 'Zilinskas', 'PI_MID_INIT': 'A', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Barbara A Zilinskas', 'EmailAddress': 'zilinskas@aesop.rutgers.edu', 'NSF_ID': '000104439', 'StartDate': '06/18/1993', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'Rutgers University New Brunswick', 'CityName': 'NEW BRUNSWICK', 'ZipCode': '089018559', 'PhoneNumber': '8489320150', 'StreetAddress': '3 RUTGERS PLZ', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'New Jersey', 'StateCode': 'NJ', 'CONGRESSDISTRICT': '12', 'CONGRESS_DISTRICT_ORG': 'NJ12', 'ORG_UEI_NUM': 'M1LVPE5GLSD9', 'ORG_LGL_BUS_NAME': 'RUTGERS, THE STATE UNIVERSITY', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1144', 'Text': 'Molecular Biophysics'}, {'Code': '9120', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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