Institution: | Department of Agricultural Biochemistry, Waite Agricultural Research Institute, University of Adelaide, Adelaide, Australia |
Abstract: | 1. NADH-benzyl viologen reductase, solubilized by acetone extraction, was purified about 10-fold from small particles of Azotobacter vinelandii. 2. The purified enzyme preparation was free from hydrogenase activity. Either NADH or NADPH served as an electron donor for the reduction of benzyl viologen. This reaction is reversible. 3. The essential thiol groups of the enzyme are protected since they do not react with N-ethylmaleimide and p-chloromercuribenzoate inhibits only after it has been preincubated with the enzyme. |