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[丙酮丁醇梭菌中NADH和NADPH-铁氧化还原蛋白氧化还原酶活性的研究]

[Study of the NADH and NADPH-ferredoxin oxidoreductase activities in Clostridium acetobutylicum].

作者信息

Petitdemange H, Cherrier C, Bengone J M, Gay R

出版信息

Can J Microbiol. 1977 Feb;23(2):152-60.

PMID:13922
Abstract

The NADH and NADPH-ferredoxin oxidoreductase have been studied in Clostridium acetobutylicum. Acetyl-CoA is an obligatory activator of NADH-ferredoxin reductase activity and NADH a competitive inhibitor of ferredoxin-NAD+ reductase activity. These regulations are the same when C. acetoburylicum moves from 'butylic-type metabolism' to 'butyric-type metabolism'; this demonstrates that NADH-ferredoxin oxidoreductase cna, through its reversible action, meet the very different cell needs imposed by these two types of culture. The physiological function of the clostridial NADPH-ferredoxin oxidoreductase was anabolic as it has been with other clostridia.

摘要

已对丙酮丁醇梭菌中的NADH和NADPH-铁氧化还原蛋白氧化还原酶进行了研究。乙酰辅酶A是NADH-铁氧化还原蛋白还原酶活性的必需激活剂,而NADH是铁氧化还原蛋白-NAD⁺还原酶活性的竞争性抑制剂。当丙酮丁醇梭菌从“丁醇型代谢”转变为“丁酸型代谢”时,这些调节作用是相同的;这表明NADH-铁氧化还原蛋白氧化还原酶可以通过其可逆作用,满足这两种培养类型所带来的截然不同的细胞需求。梭菌NADPH-铁氧化还原蛋白氧化还原酶的生理功能与其他梭菌一样,是合成代谢的。

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