[Estimation of the distance between the iron-sulfur cluster of Fe-protein and the nearest iron-sulfur cluster of Mo-Fe-protein of nitrogenase on the basis of the inductive-resonance theory of energy transfer].
The distance between fluorescein mercuric acetate (FMA), attached to the HS-group of Fe- and Mo-Fe-protein, and the nearest iron-sulphur cluster (ISC) was determined. For Fe-protein the distance was 18--20 A and for Mo-Fe-protein 12--14 A. The distance between Fe-protein FMA and the nearest Mo-protein ISC determined by complementation of the labelled Fe-protein and native Mo-Fe-protein was 14--16 A. The distance between MO-OFe-protein ISC and complement Fe-protein ISC was 18--20 A. A te-protein ISC permitted to suppose that the electron was transfered from Fe-protein ISC to Mo-Fe-protein ISC by the contact of the ISC or with the help of ATP molecule.
D001665:Binding Sites; D004735:Energy Transfer; D005452:Fluoresceins; D007501:Iron; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D008982:Molybdenum; D009591:Nitrogenase; D011485:Protein Binding; D011487:Protein Conformation
D005452:Fluoresceins; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D008982:Molybdenum; D007501:Iron; D009591:Nitrogenase
Otsenka rasstoianiia mezhdu zhelezo-sernym klasterom FE-belka i blizhaĭshim zhelezo-sernym klasterom Mo-Fe-belka nitrogenazy na osnovanii teorii induktivno-rezonansnogo perenosa énergii.