1887

Abstract

Summary: Mutants have been isolated which lack NADH-dependent nitrite reductase activity but retain NADPH-dependent sulphite reductase and formate hydrogenlyase activities. These NirB–strains synthesize cytochrome and grow normally on anaerobic glyeerol—fumarate plates. The defects map in a gene, , which is extremely close to , the gene order being Complementation studies established that and can be expressed independently. The data strongly suggest that is the structural gene for the 88 kDal NADH-dependent nitrite oxidoreductase apoprotein (EC 1.6.6.4).

The gene is apparently defective in the previously described mutant, LCB82. The mutant, LCB197, was unable to use formate as electron donor for nitrite reduction, but NADH-dependent nitrite reductase was extremely active in this strain and a normal content of cytochrome was detected. Strains carrying a or mutation gave normal rates of nitrite reduction by glucose, formate or NADH.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-131-10-2771
1985-10-01
2019-11-15
Loading full text...

Full text loading...

http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-131-10-2771
Loading
This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error