SUMMARY: A membrane-bound nitrate reductase from can utilize either sulphite or NADH as an electron donor. The sulphite-dependent nitrate reductase activity was released from the membrane by treatment with sodium deoxycholate. Cytochrome and FAD were separated from the solubilized enzyme by heat treatment and subsequent chromatography on DEAE-cellulose. The bacterial cytochrome and a preparation of horse-heart cytochrome served as electron mediators to the solubilized sulphite-dependent nitrate reductase activity with apparent values of 1.5 and 1.3 μM respectively. The NADH-linked enzymic activity, which was unstable during storage, was re-activated with reduced glutathione. It was also inactivated after treatment with deoxycholate but this effect was reversed by menadione. A possible scheme for electron transport for the sulphite- and NADH-dependent enzyme is proposed.


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