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  Structure and function of enzymes involved in the methanogenic pathway utilizing carbon dioxide and molecular hydrogen [Review]

Shima, S., Warkentin, E., Thauer, R. K., & Ermler, U. (2002). Structure and function of enzymes involved in the methanogenic pathway utilizing carbon dioxide and molecular hydrogen [Review]. Journal of Bioenergetics and Biomembranes, 93(6), 519-530. doi:10.1016/S1389-1723(02)80232-8.

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 Creators:
Shima, Seigo1, 2, Author           
Warkentin, Eberhard3, Author           
Thauer, Rudolf Kurt1, 2, Author           
Ermler, Ulrich3, Author                 
Affiliations:
1Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3135468              
2Laboratorium für Mikrobiologie, Fachbereich Biologie, Philipps-Universität, 35043 Marburg, Germany, ou_persistent22              
3Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: methanogenic archaea; methanogenesis; crystal structure; catalytic mechanism; methanofuran; tetrahydromethanopterin; F420 coenzyme M; coenzyme B; F430 NADP; nickel; metal-free hydrogenase
 Abstract: Methane is an end product of anaerobic degradation of organic compounds in fresh water environments such as lake sediments and the intestinal tract of animals. Methanogenic archaea produce methane from carbon dioxide and molecular hydrogen, acetate and C1 compounds such as methanol in an energy gaining process. The methanogenic pathway utilizing carbon dioxide and molecular hydrogen involves ten methanogen specific enzymes, which catalyze unique reactions using novel coenzymes. These enzymes have been purified and biochemically characterized. The genes encoding the enzymes have been cloned and sequenced. Recently, crystal structures of five methanogenic enzymes: formylmethanofuran: tetrahydromethanopterin formyltransferase, methenyltetrahydromethanopterin cyclohydrolase, methylenetetrahydromethanopterin reductase, F420H2:NADP oxidoreductase and methyl-coenzyme M reductase were reported. In this review, we describe the pathway utilizing carbon dioxide and molecular hydrogen and the catalytic mechanisms of the enzymes based on their crystal structures. [References: 93]

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Language(s): eng - English
 Dates: 2002-04-162002-05-172003-09-102002-06-01
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S1389-1723(02)80232-8
PMID: 16233244
 Degree: -

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Title: Journal of Bioenergetics and Biomembranes
  Other : J. Bioenerg. Biomembr.
Source Genre: Journal
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Publ. Info: New York : Plenum Press.
Pages: - Volume / Issue: 93 (6) Sequence Number: - Start / End Page: 519 - 530 Identifier: ISSN: 0145-479X
CoNE: https://pure.mpg.de/cone/journals/resource/954925473404