Premium
Formation and characterization of a transition state complex of Azotobacter vinelandii nitrogenase
Author(s) -
Duyvis Martina G.,
Wassink Hans,
Haaker Huub
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00019-1
Subject(s) - azotobacter vinelandii , nitrogenase , chemistry , characterization (materials science) , azotobacter , azotobacteraceae , nitrogen fixation , biochemistry , materials science , biology , nanotechnology , bacteria , nitrogen , organic chemistry , genetics
A stable complex is formed between the nitrogenase proteins of Azotobacter vinelandii , aluminium fluoride and MgADP. All nitrogenase activities are inhibited. The complex formation was found to be reversible. An incubation at 50°C recovers nitrogenase activity. The complex has been characterized with respect to protein and nucleotide composition and redox state of the metal‐sulphur clusters. Based on the inhibition by aluminium fluoride together with MgADP, it is proposed that a stable transition state complex of nitrogenase is isolated.