N5,N10-METHYLENETETRAHYDROMETHANOPTERIN DEHYDROGENASE FROM METHANOBACTERIUM-THERMOAUTOTROPHICUM HAS HYDROGENASE ACTIVITY

被引：132

作者：

ZIRNGIBL, C

HEDDERICH, R

THAUER, RK

机构：

[1] Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität Marburg, D-3550 Marburg, Karl-von-Frisch-Straße

来源：

FEBS LETTERS | 1990年 / 261卷 / 01期

关键词：

Coenzyme F[!sub]420[!/sub; Hydrogenase; Methanobacterium thermoautotrophicum; Methanopterin; Methylenetetrahydromethanopterin dehydrogenase; Tetrahydromethanopterin;

D O I：

10.1016/0014-5793(90)80649-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

N5,N10-Methylenetetrahydromethanopterin dehydrogenase from Methanobacterium thermoautotrophicum (strain Marburg) was purified under anaerobic conditions to apparent homogeneity and a specific activity of approximately 750 μol/min/mg protein. Polyacrylamide gel electrophoresis under native and denaturing conditions revealed that the enzyme is composed of only one polypeptide with an apparent molecular mass of 43 kDa. The purified enzyme catalyzed the dehydrogenation of N5,N10-methylenetetrahydromethanopterin (CH2H4MPT) (apparent Km20 μM) to N5,N10-methenyltetrahydromethanopterin (CHH4MPT) in the absence of any added electron acceptors. One mol of H2 was generated per mol CHH4MPT formed, indicating that protons served as electron acceptor. Coenzyme F420, NAD, NADP and viologen dyes were not reduced by CH2H4MPT. The dehydrogenase also catalyzed the reverse reaction, the reduction of CHH4MPT to CH2H4MPT with H2. The data indicate that CH2H4MPT dehydrogenase from M. thermoautotrophicum is a novel type of hydrogenase. © 1990.

引用

页码：112 / 116

页数：5

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