A salt-inhibited cytochrome c reductase obtained from the moderately halophilic bacterium, Micrococcus halodenitrificans.
A membrane-bound cytochrome c reductase from Micrococcus halodenitrificans was inhibited by NaCl at concentrations as low as 0.05 m. The inhibition was competitive with respect to cytochrome c and noncompetitive with respect to reduced nicotinamide adenine dinucleotide. Thus the effect of NaCl was to increase the apparent K(m) of the enzyme for cytochrome c and not to inhibit the intrinsic activity of the enzyme.
D002462:Cell Membrane / Q000201:enzymology; D002474:Cell-Free System; D003470:Culture Media; D003574:Cytochrome c Group / Q000378:metabolism; D006217:Halobacterium / Q000201:enzymology; D008837:Micrococcus / Q000201:enzymology* / Q000254:growth & development / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D010088:Oxidoreductases / Q000037:antagonists & inhibitors* / Q000302:isolation & purification / Q000378:metabolism; D012965:Sodium Chloride / Q000378:metabolism / Q000494:pharmacology*; D013855:Thiobacillus / Q000201:enzymology; D014733:Vibrio / Q000201:enzymology
D003470:Culture Media; D003574:Cytochrome c Group; D009243:NAD; D012965:Sodium Chloride; D010088:Oxidoreductases