“…In diazotrophic members of the K-group of Proteobacteria, to which Acetobacter diazotrophicus belongs, and in Herbaspirillum seropedicae, a L-group member, inactivation of NifA by oxygen occurs by inherent sensitivity of NifA protein to oxygen damage apparently via a Cys-aa 4 -Cys motif in the interdomain linker region [10]. Mechanisms for inactivation of NifA in ammonium-grown cells of some diazotrophs of the K-group have not been well-characterized, but in the case of A. brasilense and H. seropedicae, this occurs through the N-terminal domain of NifA, the most variable of the regions of NifA proteins [11,12]. The other NifA domains include a highly conserved central region involved in ATP hydrolysis essential for conversion of closed to open complex of RNA polymerase bound to the promoter region of NifA-activated nif/¢x genes, an interdomain linker, involved in the oxygen-dependent regulation of NifA activity [10], and a C-terminal domain, essential for the speci¢c NifA interaction with susceptible promoter sequences (reviewed in [2]).…”