PMID:9724711
| Citation |
Gardner, PR, Gardner, AM, Martin, LA and Salzman, AL (1998) Nitric oxide dioxygenase: an enzymic function for flavohemoglobin. Proc. Natl. Acad. Sci. U.S.A. 95:10378-83 |
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| Abstract |
Nitric oxide (NO*) is a toxin, and various life forms appear to have evolved strategies for its detoxification. NO*-resistant mutants of Escherichia coli were isolated that rapidly consumed NO*. An NO*-converting activity was reconstituted in extracts that required NADPH, FAD, and O2, was cyanide-sensitive, and produced NO3-. This nitric oxide dioxygenase (NOD) contained 19 of 20 N-terminal amino acids identical to those of the E. coli flavohemoglobin. Furthermore, NOD activity was produced by the flavohemoglobin gene and was inducible by NO*. Flavohemoglobin/NOD-deficient mutants were also sensitive to growth inhibition by gaseous NO*. The results identify a function for the evolutionarily conserved flavohemoglobins and, moreover, suggest that NO* detoxification may be a more ancient function for the widely distributed hemoglobins, and associated methemoglobin reductases, than dioxygen transport and storage. |
| Links | |
| Keywords |
Amino Acid Sequence; Bacterial Proteins/metabolism; Base Sequence; Cell-Free System; Chromatography, Ion Exchange; DNA Primers; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Escherichia coli/genetics; Hemeproteins/metabolism; Molecular Sequence Data; Mutation; Oxygenases/chemistry; Oxygenases/metabolism |
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