Nitrobacter hamburgensis

Saccharomyces cerevisiae Mucor c ircinelloides Gallus gallus Xenopus laevis Homo sapiens Mus musculus Bradyrhizobium japonicum Nitrobacter hamburgensi Bradyrhizobium sp. BTAil Azotobacter vinelandii Shewane1la ama zonensis Conserved sites Conserved sites (plants)... 

Many nitrite-oxidizing bacteria have been discovered, for example Nitrobacter winogradskyi, Nitrobacter hamburgensis, Nitrospina gracilis, Nitrococcus mobilis, and Nitrospira marina, (Watson et al., 1989). Among them, N. winogradskyi is studied most extensively. 

Nitrite oxidoreductase has been purified also from Nitrobacter hamburgensis (Sundermeyer-Klinger et al., 1984) and Nitrospira moscoviensis (Spieck et al., 1998). The N. hamburgensis enzyme has been reported to have heme C but not to have heme A. It does not catalyze the reduction of horse ferricytochrome c with nitrite although it catalyzes the reduction of ferricyanide. The N. moscoviensis enzyme has been reported to have heme B but not to have either heme A or heme C. Although the N. moscoviensis enzyme catalyzes the oxidation of nitrite with chlorate as the electron acceptor, it has not been reported whether cytochrome c or ferricyanide acts as the electron acceptor for the enzyme. The enzyme of this bacterium is known to be located in the periplasmic space. Table 3.3 lists some properties of nitrite oxidoreductase purified from three species of the nitrite-oxidizing bacteria. 

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