Two NADH:ubiquinone oxidoreductases of Azotobacter vinelandii and their role in the respiratory protection
1998
Initial steps of the Azotobacter vinelandii respiratory chain have been studied on the inside-out subcellular vesicles. Two NADH:ubiquinone oxidoreductases were revealed: (i) proton-motive, capsaicin-sensitive and oxidizing dNADH as well as NADH enzyme and (ii) enzyme non-coupled to the energy conservation, capsaicin-resistant and oxidizing only NADH. The level of the oxidoreductases strongly depends upon [O2] and [NH3] in the growth medium. Increase in [O2] results in lowering of the coupled-enzyme level and in rise of the non-coupled one. Exclusion of NH3 from the growth medium increases the level of the non-coupled enzyme whereas that of the coupled enzyme remains constant. The O2-linked control of NADH:ubiquinone oxidoreductases requires CydR, a Fnr-like regulatory protein. Summarizing the above observations with those made in this group on the terminal steps of the A. vinelandii respiratory chains, one can assume that the respiratory protection of nitrogenase could be carried out by co-operation of the non-coupled NADH:ubiquinone oxidoreductase and the "partially coupled" quinoloxidase of the bd-type. Efficiency of this chain seems to be five-fold lower than that of the usual proton-motive chain (the coupled NADH:ubiquinone oxidoreductase, the Q-cycle and cytochrome oxidase of the O-type) which is also present in A. vinelandii and operates at low [O2].
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