Enzymology of the Hydroxylamine Oxidizing System of         Nitrosomonas
{'Code': '08070400', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'MCB', 'LongName': 'Div Of Molecular and Cellular Bioscience'}}
{'SignBlockName': 'Marcia Steinberg', 'PO_EMAI': None, 'PO_PHON': None}
In soils, fertililzer ammonia is oxidized to nitrite (NH3+1.5                   02-->HNO2+H20) by the chemautotrophic nitrifying bacterium                      Nitrosomonas europaea.  Nitrite is oxidized by Nitrobacter to                   nitrate, a primary source of N for food protein in non-                         leguminous crops.  Thus the initial transformation of most                      food ntirogen is carried out by Nitrosomonas.  Of great                         economic importance is loss of N in soils, as N-gases                           produced by Nitrosomonas during oxidation of NH3 or by                          reduction of nitrate by denitrifying bacteria.  Control of                      agricultural loss by denitrification is attempted by the use                    of inhibitors of ammonia oxidation by Nitrosomonas.  This                       lends significance to improved knowledge of the mechanism of                    ammonia oxidation.                                                                                                                                              NH3 is oxygenated by O2 to NH2OH which is then oxidized                         (NH2OH+H2)-->HNO2+4e-+4H+) by the enzyme hydroxcylamine                         oxidoreductase, "HAO."  HAO is a large ( 200 Kd) and                            unusually complex hemoprotein  ( 24 c hemes and  3 substrate                    binding "P460" groups).  Two electrons pass from HAO,                           in an electron transport chain which includes the tetraheme                     cytochrome c554 and other unknown components, to a membrane                     terminal oxidase.  Two additional electrons pass from HAO to                    the ammonia monoxygenase.  Goals of the project include:                        determination of the subunit structure and amino acid sequence                  of HAO, the ring structure of P460 of HAO and the structure                     of the substrate binding site and identification of the                         electron exit site of HAO;  determination of the amino acid                     sequence and electron entry and exit sites of cytochrome c-                     554; and reconstitution of HAO with the terminal oxidase.                       The approach involves enzymology, protein chemistry, optical                    and EPR spectroscopy rapid kinetics, cloning and DNA sequencing.
{'FirstName': 'Alan', 'LastName': 'Hooper', 'PI_MID_INIT': 'B', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'Alan B Hooper', 'EmailAddress': 'hooper@cbs.umn.edu', 'PI_PHON': '6126244930', 'NSF_ID': '000322864', 'StartDate': '01/01/1988', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of Minnesota Saint Paul', 'CityName': 'Minneapolis', 'ZipCode': '554552000', 'PhoneNumber': '6126252435', 'StreetAddress': '450 University Gateway', 'StreetAddress2': '200 Oak Street SE', 'CountryName': 'United States', 'StateName': 'Minnesota', 'StateCode': 'MN', 'CONGRESSDISTRICT': '05', 'CONGRESS_DISTRICT_ORG': 'MN05', 'ORG_UEI_NUM': None, 'ORG_LGL_BUS_NAME': None, 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '1108', 'Text': 'INSTRUMENTAT & INSTRUMENT DEVP'}, {'Code': '1144', 'Text': 'Molecular Biophysics'}, {'Code': '9120', 'Text': 'CROSS-DIRECTORATE PROGRAMS'}, {'Code': '9145', 'Text': 'SPECIAL PROGRAMS-RESERVE'}]
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