Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Nature of the oxidation-reduction properties of nitrite reductase from Desulfovibrio desulfuricans

Journal Article · · Biochem. Biophys. Res. Commun.; (United States)
Nitrite reductase as isolated from Desulfovibrio desulfuricans shows a complex set of rhombically distorted high-spin ferric heme and low-spin ferric heme resonances at 11/sup 0/K. These resonances disappear on enzymatic reduction with hydrogen, hydrogenase from D. vulgaris and FAD as redox mediator. The addition of nitrite to the reduced enzyme results in reoxidation of nitrite reductase as evidenced by the reappearance of most of the initial signal intensities of high-spin and low-spin ferric heme resonances. Simultaneously an intense and unusual broadened signal appears in the g = 2 region, suggesting the formation of a novel heme-nitric oxide signal with the main g-value at 2.08. Confirmation of this heme-nitric oxide complex was demonstrated by reoxidation of reduced enzyme with /sup 15/NO/sub 2//sup -1/ instead of /sup 14/NO/sub 2//sup -1/ resulting in a decrease from three to two of the hyperfine interaction pattern of nitrogen. Thus nitrite reduction to ammonia by nitrite reductase occurs via a heme-nitric oxide intermediate as reported with spinach nitrite reductase.
Research Organization:
Univ. of Georgia, Athens
DOE Contract Number:
AS09-79ER10499
OSTI ID:
5729634
Journal Information:
Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Journal Issue: 1 Vol. 96:1; ISSN BBRCA
Country of Publication:
United States
Language:
English