H sub(2)-Forming methylenetetrahydro-methanopterin dehydrogenase, a novel type of hydrogenase without iron-sulfur clusters in methanogenic archaea

A novel hydrogenase has recently been found in methanogenic archaea. It catalyzes the reversible dehydrogenation of methylenetetrahydro-methanopterin (CH sub(2) = H sub(4) MPT) to methenyltetrahydro-methanopterin (CH identical with H sub(4)MPT super(+)) and H sub(2) and was therefore named H sub(2)-...

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Published inEuropean journal of biochemistry Vol. 208; no. 2; pp. 511 - 520
Main Authors Zirngibl, C, van Dongen, W, Schwoerer, B, von Buenau, R, Richter, M, Klein, A, Thauer, R K
Format Journal Article
LanguageEnglish
Published 01.01.1992
Subjects
biosynthesis
characterization
hydrogen
Methanobacterium thermoautotrophicum
methylenetetrahydromethanopterin dehydrogenase
purification
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Summary:A novel hydrogenase has recently been found in methanogenic archaea. It catalyzes the reversible dehydrogenation of methylenetetrahydro-methanopterin (CH sub(2) = H sub(4) MPT) to methenyltetrahydro-methanopterin (CH identical with H sub(4)MPT super(+)) and H sub(2) and was therefore named H sub(2)-forming methylenetetrahydro-methanopterin dehydrogenase. We report here that the purified enzyme from Methanobacterium thermoautotrophicum) exhibits the following other unique properties: (a) the colorless protein; (b) the activity was not inhibited by carbon monoxide, acetylene, nitrite, cyanide, or azide; (c) the enzyme did not catalyze an isotopic exchange between super(3)H sub(2) and super(1)H super(+).
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ISSN:0014-2956