Association of hydrogenase and dithionite reductase activities with the nitrite reductase of Desulfovibrio desulfuricans

Journal Article · Wed May 14 04:00:00 EDT 1980 · Biochem. Biophys. Res. Commun.; (United States)

DOI:https://doi.org/10.1016/S0006-291X(80)80184-7· OSTI ID:5764997

Steenkamp, D J; Peck, Jr, H D

The membrane bound respiratory nitrite reductase from Desulfovibrio desulfuricans contains six c-type heme groups and catalyzes the six electron reduction of nitrite to ammonia. The purified enzyme required an excess of reducing equivalents for reduction relative to the amount of nitrite consumed in its reoxidation. The anomaly could be accounted for in terms of the presence of low levels of dithionite reductase and hydrogenase activity in the preparation. Dithionite reductase may be an alternate activity of nitrite reductase, whereas hydrogenase was shown to be a contaminant. The contaminating hydrogenase used nitrite reductase as electron acceptor in preference to cytochrome c/sub 3/ or benzyl viologen.

• Research Organization: Univ. of Georgia, Athens
• OSTI ID: 5764997
• Journal Information: Biochem. Biophys. Res. Commun.; (United States), Journal Name: Biochem. Biophys. Res. Commun.; (United States) Vol. 94:1; ISSN BBRCA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
550700 -- Microbiology
59 BASIC BIOLOGICAL SCIENCES
AMMONIA
BACTERIA
BIOCHEMISTRY
CHEMICAL PROPERTIES
CHEMICAL REACTIONS
CHEMISTRY
CYTOCHROMES
DESULFOVIBRIO
ENZYME ACTIVITY
ENZYMES
HYDRIDES
HYDROGEN COMPOUNDS
HYDROGENASES
MICROORGANISMS
NITRITES
NITRO-GROUP DEHYDROGENASES
NITROGEN COMPOUNDS
NITROGEN HYDRIDES
OXIDOREDUCTASES
OXYGEN COMPOUNDS
PIGMENTS
REDUCTION