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Appl. Environ. Microbiol., Jul 1997, 2613-2618, Vol 63, No. 7
Copyright © 1997, American Society for Microbiology

Physiology and Enzymology Involved in Denitrification by Shewanella putrefaciens

B Krause and KH Nealson
Center for Great Lakes Studies, University of Wisconsin-Milwaukee, Milwaukee, Wisconsin 53204

Nitrate reduction to N(inf2)O was investigated in batch cultures of Shewanella putrefaciens MR-1, MR-4, and MR-7. All three strains reduced nitrate to nitrite to N(inf2)O, and this reduction was coupled to growth, whereas ammonium accumulation was very low (0 to 1 (mu)mol liter(sup-1)). All S. putrefaciens isolates were also capable of reducing nitrate aerobically; under anaerobic conditions, nitrite levels were three- to sixfold higher than those found under oxic conditions. Nitrate reductase activities (31 to 60 (mu)mol of nitrite min(sup-1) mg of protein(sup-1)) detected in intact cells of S. putrefaciens were equal to or higher than those seen in Escherichia coli LE 392. K(infm) values for nitrate reduction ranged from 12 mM for MR-1 to 1.3 mM for MR-4 with benzyl viologen as an artifical electron donor. Nitrate and nitrite reductase activities in cell-free preparations were demonstrated in native gels by using reduced benzyl viologen. Detergent treatment of crude and membrane extracts suggested that the nitrate reductases of MR-1 and MR-4 are membrane bound. When the nitrate reductase in MR-1 was partially purified, three subunits (90, 70, and 55 kDa) were detected in denaturing gels. The nitrite reductase of MR-1 is also membrane bound and appeared as a 60-kDa band in sodium dodecyl sulfate-polyacrylamide gels after partial purification.

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