Periplasmic cytochrome C552 of Escherichia coli K12. Oligomeric structure and its role in nitrite reduction.
Perisplasmic cytochrome C552 was purified from a cold shock fluid. We demonstrated that this protein could reduce nitrite into ammonium. The reducing equivalents could be donated by formate or NADH through some segment of the membrane respiratory chain. FAD addition was necessary when pure cytochrome was used to reduce nitrite. The predominant form was found to have a molecular weight of about 65 to 70 K daltons, composed of three 21,000 d. subunits. Hemes may or may not be present on the subunit.
D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003574:Cytochrome c Group / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D006859:Hydrogen / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D009572:Nitrite Reductases / Q000378:metabolism; D009573:Nitrites / Q000378:metabolism*
D003574:Cytochrome c Group; D046911:Macromolecular Substances; D009573:Nitrites; C083951:cytochrome c553; D006859:Hydrogen; C022302:cytochrome C-552; D009572:Nitrite Reductases