Formation and characterization of a transition state complex of Azotobacter vinelandii nitrogenase

FEBS Letters

Duyvis, Martina G.¹  Wassink, Hans¹  Haaker, Huub¹ 

[1] Department of Biochemistry, Agricultural University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands

关键词: Nitrogenase (Azotobacter vinelandii);    ATP-analogue;    Aluminium fluoride;    Molecular switch protein;    Av1;    MoFe protein and Fe protein from Azotobacter vinelandii nitrogenase;    Av2;    MoFe protein and Fe protein from Azotobacter vinelandii nitrogenase;    Kp1;    MoFe protein and Fe protein from Klebsiella pneumoniae nitrogenase;    Kp2;    MoFe protein and Fe protein from Klebsiella pneumoniae nitrogenase;   

DOI  :  10.1016/0014-5793(96)00019-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown