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大肠杆菌K-12硝酸还原酶中的一个紫外线敏感靶点。

An ultraviolet light sensitive target in nitrate reductase of Escherichia coli K-12.

作者信息

Francisco R, Brito C, Dubourdieu M

机构信息

Grupo de Biología Experimental, Facultad de Ciencias, Universidad de Los Andes, Mérida, Venezuela.

出版信息

Biochem Int. 1987 Dec;15(6):1079-88.

PMID:3326602
Abstract

Ultraviolet light was shown to inactivate purified nitrate reductase in the presence of reduced benzyl viologen. Loss of activity was not complete, reaching 60 to 70%. Photolysis was maximum at 345 nm. The differential spectrum between native and irradiated enzyme exhibited absorption bands at 216, 275, 314 and 365 nm. The photosensitive electron carrier could be extracted by organic solvents. It had the following absorption bands: 225, 275 and 285 nm. It was reduced by Nile blue A but not by methylene blue. The precise nature of this light sensitive molecule could not be determined although the results support the idea that this chromophore might be a naphthoquinone.

摘要

在还原型苄基紫精存在的情况下,紫外线可使纯化的硝酸还原酶失活。活性丧失并不完全,达到60%至70%。光解在345纳米处达到最大值。天然酶和辐照酶之间的差分光谱在216、275、314和365纳米处显示出吸收带。光敏电子载体可用有机溶剂萃取。它具有以下吸收带:225、275和285纳米。它可被尼罗蓝A还原,但不能被亚甲蓝还原。尽管结果支持这种发色团可能是萘醌的观点,但这种光敏分子的确切性质尚无法确定。

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引用本文的文献

1
Isolation and identification of menaquinone-9 from purified nitrate reductase of Escherichia coli.从大肠杆菌纯化的硝酸还原酶中分离并鉴定甲基萘醌-9
J Bacteriol. 1995 Jul;177(13):3728-35. doi: 10.1128/jb.177.13.3728-3735.1995.