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The tandem domain rhodanese-homology protein RhdA of  Azotobacter vinelandii  shows an active-site loop structure that confers structural peculiarity in the environment of its catalytic cysteine residue. The  in vivo  effects of the lack of RhdA were investigated using an  A. vinelandii  mutant strain (MV474) in which the  rhdA  gene was disrupted by deletion. Here, by combining analytical measurements and transcript profiles, we show that deletion of the  rhdA  gene generates an oxidative stress condition to which  A. vinelandii  responds by activating defensive mechanisms. In conditions of growth in the presence of the superoxide generator phenazine methosulfate, a stressor-dependent induction of  rhdA  gene expression was observed, thus highlighting that RhdA is important for  A. vinelandii  to sustain oxidative stress. The potential of RhdA to buffer general levels of oxidants in  A. vinelandii  cells via redox reactions involving its cysteine thiol is discussed.

The rhodanese RhdA helps Azotobacter vinelandii in maintaining cellular redox balance