Carpenter C E, Reddy D S, Cornforth D P
Appl Environ Microbiol. 1987 Mar;53(3):549-52. doi: 10.1128/aem.53.3.549-552.1987.
Clostridial ferredoxin and pyruvate-ferredoxin oxidoreductase activity was investigated after in vitro or in vivo treatment with sodium nitrite. In vitro treatment of commercially available Clostridium pasteurianum ferredoxin with sodium nitrite inhibited ferredoxin activity. Inhibition of ferredoxin activity increased with increasing levels of sodium nitrite. Ferredoxin was isolated from normal C. pasteurianum and Clostridium botulinum cultures and from cultures incubated with 1,000 micrograms of sodium nitrite per ml for 45 min. The activity of in vivo nitrite-treated ferredoxin was decreased compared with that of control ferredoxin. Pyruvate-ferredoxin oxidoreductase isolated from C. botulinum cultures incubated with 1,000 micrograms of sodium nitrite per ml showed less activity than did control oxidoreductase. It is concluded that the antibotulinal activity of nitrite is due at least in part to inactivation of ferredoxin and pyruvate-ferredoxin oxidoreductase.
在用亚硝酸进行体外或体内处理后,对梭菌铁氧化还原蛋白和丙酮酸-铁氧化还原蛋白氧化还原酶活性进行了研究。用亚硝酸对市售巴氏固氮梭菌铁氧化还原蛋白进行体外处理会抑制铁氧化还原蛋白活性。随着亚硝酸水平的升高,铁氧化还原蛋白活性的抑制作用增强。从正常的巴氏固氮梭菌和肉毒梭菌培养物以及每毫升含1000微克亚硝酸孵育45分钟的培养物中分离出铁氧化还原蛋白。与对照铁氧化还原蛋白相比,体内经亚硝酸盐处理的铁氧化还原蛋白活性降低。从每毫升含1000微克亚硝酸孵育的肉毒梭菌培养物中分离出的丙酮酸-铁氧化还原蛋白氧化还原酶的活性低于对照氧化还原酶。得出的结论是,亚硝酸盐的抗肉毒杆菌活性至少部分归因于铁氧化还原蛋白和丙酮酸-铁氧化还原蛋白氧化还原酶的失活。