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 in | European journal of biochemistry Vol. 208; no. 2; pp. 511 - 520 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
01.01.1992
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Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-2 |
ISSN: | 0014-2956 |