H2‐forming methylenetetrahydromethanopterin 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 methylenetetrahydromethanopterin (CH2─H4MPT) to methenyltetrahydromethanopterin (CH═H4MPT+) and H2 and was therefore named H2‐forming methylenetetrahydromethanopterin dehydrogenase. Th...

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Veröffentlicht in:European journal of biochemistry 1992-09, Vol.208 (2), p.511-520
Hauptverfasser: ZIRNGIBL, Carmen, DONGEN, Walter, SCHWÖRER, Beatrix, BÜNAU, Rudolf, RICHTER, Monika, KLEIN, Albrecht, THAUER, Rudolf K.
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container_issue 2
container_start_page 511
container_title European journal of biochemistry
container_volume 208
creator ZIRNGIBL, Carmen
DONGEN, Walter
SCHWÖRER, Beatrix
BÜNAU, Rudolf
RICHTER, Monika
KLEIN, Albrecht
THAUER, Rudolf K.
description A novel hydrogenase has recently been found in methanogenic archaea. It catalyzes the reversible dehydrogenation of methylenetetrahydromethanopterin (CH2─H4MPT) to methenyltetrahydromethanopterin (CH═H4MPT+) and H2 and was therefore named H2‐forming methylenetetrahydromethanopterin dehydrogenase. The hydrogenase, which is composed of only one polypeptide with an apparent molecular mass of 43 kDa, does not mediate the reduction of viologen dyes with either H2 or CH2─H4MPT. We report here that the purified enzyme from Methanobacterium thermoautotrophicum exhibits the following other unique properties: (a) the colorless protein with a specific activity of 2000 U/mg (Vmax) did not contain iron‐sulfur clusters, nickel, or flavins; (b) the activity was not inhibited by carbon monoxide, acetylene, nitrite, cyanide, or azide; (c) the enzyme did not catalyze an isotopic exchange between 3H2 and 1H+; (d) the enzyme catalyzed the reduction of CH═H4MPT+ with 3H2 generating [methylene‐3H]CH2─H4MPT; and (e) the primary structure contained at most four conserved cysteines as revealed by a comparison of the DNA‐deduced amino acid sequence of the proteins from M. thermoautotrophicum and Methanopyrus kandleri. None of the four cysteines were closely spaced as would be indicative for a (NiFe) hydrogenase or a ferredoxintype iron‐sulfur protein. Properties of the H2‐forming methylenetetrahydromethanopterin dehydrogenase from Methanobacterium wolfei are also described indicating that the enzyme from this methanogenic archaeon is very similar to the enzyme from M. thermoautotrophicum with respect both to molecular and catalytic properties.
doi_str_mv 10.1111/j.1432-1033.1992.tb17215.x
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We report here that the purified enzyme from Methanobacterium thermoautotrophicum exhibits the following other unique properties: (a) the colorless protein with a specific activity of 2000 U/mg (Vmax) did not contain iron‐sulfur clusters, nickel, or flavins; (b) the activity was not inhibited by carbon monoxide, acetylene, nitrite, cyanide, or azide; (c) the enzyme did not catalyze an isotopic exchange between 3H2 and 1H+; (d) the enzyme catalyzed the reduction of CH═H4MPT+ with 3H2 generating [methylene‐3H]CH2─H4MPT; and (e) the primary structure contained at most four conserved cysteines as revealed by a comparison of the DNA‐deduced amino acid sequence of the proteins from M. thermoautotrophicum and Methanopyrus kandleri. None of the four cysteines were closely spaced as would be indicative for a (NiFe) hydrogenase or a ferredoxintype iron‐sulfur protein. 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It catalyzes the reversible dehydrogenation of methylenetetrahydromethanopterin (CH2─H4MPT) to methenyltetrahydromethanopterin (CH═H4MPT+) and H2 and was therefore named H2‐forming methylenetetrahydromethanopterin dehydrogenase. The hydrogenase, which is composed of only one polypeptide with an apparent molecular mass of 43 kDa, does not mediate the reduction of viologen dyes with either H2 or CH2─H4MPT. 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Properties of the H2‐forming methylenetetrahydromethanopterin dehydrogenase from Methanobacterium wolfei are also described indicating that the enzyme from this methanogenic archaeon is very similar to the enzyme from M. thermoautotrophicum with respect both to molecular and catalytic properties.</description><subject>Amino Acid Sequence</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Catalysis</subject><subject>Cyanides - pharmacology</subject><subject>Cysteine - analysis</subject><subject>Flavins - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydrogen - metabolism</subject><subject>Iron-Sulfur Proteins - analysis</subject><subject>Metabolism. 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Psychology</topic><topic>Hydrogen - metabolism</topic><topic>Iron-Sulfur Proteins - analysis</topic><topic>Metabolism. Enzymes</topic><topic>Methanobacterium - enzymology</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Nickel - analysis</topic><topic>Oxidation-Reduction</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - chemistry</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - genetics</topic><topic>Oxidoreductases Acting on CH-NH Group Donors - metabolism</topic><topic>Oxygen - pharmacology</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Spectrophotometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>ZIRNGIBL, Carmen</creatorcontrib><creatorcontrib>DONGEN, Walter</creatorcontrib><creatorcontrib>SCHWÖRER, Beatrix</creatorcontrib><creatorcontrib>BÜNAU, Rudolf</creatorcontrib><creatorcontrib>RICHTER, Monika</creatorcontrib><creatorcontrib>KLEIN, Albrecht</creatorcontrib><creatorcontrib>THAUER, Rudolf K.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>European journal of biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>ZIRNGIBL, Carmen</au><au>DONGEN, Walter</au><au>SCHWÖRER, Beatrix</au><au>BÜNAU, Rudolf</au><au>RICHTER, Monika</au><au>KLEIN, Albrecht</au><au>THAUER, Rudolf K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>H2‐forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron‐sulfur clusters in methanogenic archaea</atitle><jtitle>European journal of biochemistry</jtitle><addtitle>Eur J Biochem</addtitle><date>1992-09</date><risdate>1992</risdate><volume>208</volume><issue>2</issue><spage>511</spage><epage>520</epage><pages>511-520</pages><issn>0014-2956</issn><eissn>1432-1033</eissn><coden>EJBCAI</coden><abstract>A novel hydrogenase has recently been found in methanogenic archaea. It catalyzes the reversible dehydrogenation of methylenetetrahydromethanopterin (CH2─H4MPT) to methenyltetrahydromethanopterin (CH═H4MPT+) and H2 and was therefore named H2‐forming methylenetetrahydromethanopterin dehydrogenase. The hydrogenase, which is composed of only one polypeptide with an apparent molecular mass of 43 kDa, does not mediate the reduction of viologen dyes with either H2 or CH2─H4MPT. We report here that the purified enzyme from Methanobacterium thermoautotrophicum exhibits the following other unique properties: (a) the colorless protein with a specific activity of 2000 U/mg (Vmax) did not contain iron‐sulfur clusters, nickel, or flavins; (b) the activity was not inhibited by carbon monoxide, acetylene, nitrite, cyanide, or azide; (c) the enzyme did not catalyze an isotopic exchange between 3H2 and 1H+; (d) the enzyme catalyzed the reduction of CH═H4MPT+ with 3H2 generating [methylene‐3H]CH2─H4MPT; and (e) the primary structure contained at most four conserved cysteines as revealed by a comparison of the DNA‐deduced amino acid sequence of the proteins from M. thermoautotrophicum and Methanopyrus kandleri. None of the four cysteines were closely spaced as would be indicative for a (NiFe) hydrogenase or a ferredoxintype iron‐sulfur protein. Properties of the H2‐forming methylenetetrahydromethanopterin dehydrogenase from Methanobacterium wolfei are also described indicating that the enzyme from this methanogenic archaeon is very similar to the enzyme from M. thermoautotrophicum with respect both to molecular and catalytic properties.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>1521540</pmid><doi>10.1111/j.1432-1033.1992.tb17215.x</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record>
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ispartof European journal of biochemistry, 1992-09, Vol.208 (2), p.511-520
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subjects Amino Acid Sequence
Bacteriology
Base Sequence
Biological and medical sciences
Catalysis
Cyanides - pharmacology
Cysteine - analysis
Flavins - analysis
Fundamental and applied biological sciences. Psychology
Hydrogen - metabolism
Iron-Sulfur Proteins - analysis
Metabolism. Enzymes
Methanobacterium - enzymology
Microbiology
Molecular Sequence Data
Nickel - analysis
Oxidation-Reduction
Oxidoreductases Acting on CH-NH Group Donors - chemistry
Oxidoreductases Acting on CH-NH Group Donors - genetics
Oxidoreductases Acting on CH-NH Group Donors - metabolism
Oxygen - pharmacology
Sequence Homology, Nucleic Acid
Spectrophotometry
title H2‐forming methylenetetrahydromethanopterin dehydrogenase, a novel type of hydrogenase without iron‐sulfur clusters in methanogenic archaea
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