MacGregor C H, Schnaitman C A
J Bacteriol. 1972 Oct;112(1):388-91. doi: 10.1128/jb.112.1.388-391.1972.
Acid-treated extracts of Escherichia coli were tested for their ability to restore reduced nicotinamide adenine dinucleotide phosphate-nitrate reductase activity to an extract of a Neurospora nit-1 mutant which produces a defective enzyme. With wild-type E. coli this complementation activity was more readily detected in the cytoplasmic fraction, although the nitrate reductase activity was found primarily in the particulate fraction. chlB mutants of E. coli appeared to have more complementation activity in the cytoplasm than was observed in the wild type, but no activity in the particulate fraction. The other chl mutants had little or no activity in either fraction. These results suggest that chlB mutants can produce a component or cofactor which is missing in the other mutants and in the Neurospora mutant, but cannot transfer it to the nitrate reductase enzyme.
对经酸处理的大肠杆菌提取物进行了测试,以检测其将还原型烟酰胺腺嘌呤二核苷酸磷酸 - 硝酸盐还原酶活性恢复至产生缺陷酶的粗糙脉孢菌nit - 1突变体提取物的能力。对于野生型大肠杆菌,尽管硝酸盐还原酶活性主要存在于颗粒部分,但这种互补活性在细胞质部分中更容易检测到。大肠杆菌的chlB突变体在细胞质中似乎比野生型具有更多的互补活性,但在颗粒部分没有活性。其他chl突变体在这两个部分中几乎没有或没有活性。这些结果表明,chlB突变体可以产生其他突变体和粗糙脉孢菌突变体中缺失的一种成分或辅因子,但不能将其转移到硝酸盐还原酶中。