On the cyclitol oxidizing enzyme system of Acetobacter suboxydans.

The oxidation of various inositols (hexahydroxycyclohexanes) and quercitols (pentahydroxycyclohexanes) and their derivatives by resting cells of Acetobacter suboxydans has been studied by Chargaff and his students (1, 2), who found that the specificity exhibited by the organism toward the cyclitols studied was not adequately described by the Bertrand-Hudson rules (3) for open chain polyalcohols. This led the Columbia workers to formulate new rules describing the steric requirements for cyclitol oxidation, in so far as these could be ascertained with the substrates available. More recently, Posternak and Reymond (4) have repeated Chargaff’s work and extended it to the cyclohexanetetrols, the cyclohexanetriols, and lower cyclic alcohols. The Swiss workers, who used a Delft strain of A. suboxydaas, largely confirmed the earlier observations on the inositols and quercitols, but found that the oxidation of the tetrols and lower alcohols did not seem to follow either the Bertrand-Hudson or the Chargaff rules consistently. The experiments with cyclitol oxidation which have been carried out in the authors’ laboratory during the last 3 years involve a number of compounds not previously reported. In addition, use has been made of the cell-free preparation of Acetobacter enzymes described by Franz1 and Chargaff (5). The results obtained help to define some of the limitations of Chargaff’s rules as they apply to the higher cyclitols, and provide an explanation for the supposedly anomalous behavior of 1, cis-2, cis-3-cyclohexanetriol (y-cyclohexanetriol), which had earlier been studied by Posternak and Ravenna (6).