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Position of the ATP-binding site of the Fe-protein relative to the iron-sulfur clusters 4Fe-4S and the iron-molybdenum-containing cofactor

Journal Article · · Biochemistry (Engl. Transl.); (United States)
OSTI ID:5879468
; ;
Nitrogenase was affinity labeled with epsilon-ATP at the ATP-binding sites and separated into protein components by ion exchange chromatography. In spectrofluorometric titration of the labeled Fe-protein with the native MoFe-protein from the wild strain of Azotobacter and the MoFe-protein not containing iron-sulfur clusters 4Fe-4S, a 4-6-fold quenching of the fluorescence of immobilized epsilon-ATP was observed. When the labeled Fe-protein was titrated with MoFe-protein from the Azotobacter mutant UW-45, on the contrary, there was a four-fold increase in the fluorescence of immobilized epsilon-ATP. Since the MoFe-protein of the Azotobacter mutant UW-45 differs from the MoFe-protein from the wild strain of Azotobacter only by the absence of an iron-molybdenum-containing cofactor (Fe-Mo-cofactor), it is suggested that the ATP-binding site of the Fe-protein is situated next to the FeMo-cofactor and at a distance from the iron-sulfur clusters 4Fe-4S when a complex is formed with the MoFe-protein. The formation of a complex is accompanied by a change in the conformation of the Fe-protein.
Research Organization:
Institute of Chemical Physics, Chernogolovka, USSR
OSTI ID:
5879468
Journal Information:
Biochemistry (Engl. Transl.); (United States), Journal Name: Biochemistry (Engl. Transl.); (United States) Vol. 50:12; ISSN BIORA
Country of Publication:
United States
Language:
English

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Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
400102 -- Chemical & Spectral Procedures
400105 -- Separation Procedures
550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ABSORPTION SPECTRA
ATP
AZOTOBACTER
BACTERIA
BIOCHEMISTRY
CELL CULTURES
CHEMICAL ANALYSIS
CHEMISTRY
CHROMATOGRAPHY
COMPLEXOMETRY
ELECTRON TRANSFER
EMISSION SPECTROSCOPY
ENZYME ACTIVITY
ENZYMES
FLUORESCENCE
FLUORESCENCE SPECTROSCOPY
ION EXCHANGE CHROMATOGRAPHY
IRON COMPOUNDS
LUMINESCENCE
MEMBRANE PROTEINS
MICROORGANISMS
MOLYBDENUM COMPOUNDS
NITRO-GROUP DEHYDROGENASES
NITROGENASE
NUCLEOTIDES
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PROTEINS
QUANTITATIVE CHEMICAL ANALYSIS
RECEPTORS
REFRACTORY METAL COMPOUNDS
SEPARATION PROCESSES
SPECTRA
SPECTROSCOPY
SULFUR COMPOUNDS
TRANSITION ELEMENT COMPOUNDS