Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Function of methanofuran, tetrahydromethanopterin, and coenzyme F 420 in Archaeoglobus fulgidus

Function of methanofuran, tetrahydromethanopterin, and coenzyme F 420 in Archaeoglobus fulgidus 203 152 152 4 4 D. Möller-Zinkhan G. Börner R. K. Thauer Laboratorium für Mikrobiologie, FB Biologie Philipps-Universität Karl-von-Frisch-Strasse D-3550 Marburg Germany Abstract Archaeoglobus fulgidus is an extremely thermophilic archaebacterium that can grow at the expense of lactate oxidation with sulfate to CO 2 and H 2 S. The organism contains coenzyme F 420 , tetrahydromethanopterin, and methanofuran which are coenzymes previously thought to be unique for methanogenic bacteria. We report here that the bacterium contains methylenetetrahydromethanopterin: F 420 oxidoreductase (20 U/mg), methenyltetrahydromethanopterin cyclohydrolase (0.9 U/mg), formyltetrahydromethanopterin: methanofuran formyltransferase (4.4 U/mg), and formylmethanofuran: benzyl viologen oxidoreductase (35 mU/mg). Besides these enzymes carbon monoxide: methyl viologen oxidoreductase (5 U/mg), pyruvate: methyl viologen oxidoreductase (0.7 U/mg), and membranebound lactate: dimethylnaphthoquinone oxidoreductase (0.1 U/mg) were found. 2-Oxoglutarate dehydrogenase, which is a key enzyme of the citric acid cycle, was not detectable. From the enzyme outfit it is concluded that in A. fulgidus lactate is oxidized to CO 2 via a modified acetyl-CoA/carbon monoxide dehydrogenase pathway involving C 1 -intermediates otherwise only used by methanogenic bacteria. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Microbiology Springer Journals

Function of methanofuran, tetrahydromethanopterin, and coenzyme F 420 in Archaeoglobus fulgidus

Download PDF
7 pages

Loading next page...
 
/lp/springer-journals/function-of-methanofuran-tetrahydromethanopterin-and-coenzyme-f-420-in-I4XBvYYI90

References (48)

Publisher
Springer Journals
Copyright
Copyright © 1989 by Springer-Verlag
Subject
Life Sciences; Biotechnology; Biochemistry, general; Cell Biology; Ecology; Microbial Ecology; Microbiology
ISSN
0302-8933
eISSN
1432-072X
DOI
10.1007/BF00425174
Publisher site
See Article on Publisher Site

Abstract

203 152 152 4 4 D. Möller-Zinkhan G. Börner R. K. Thauer Laboratorium für Mikrobiologie, FB Biologie Philipps-Universität Karl-von-Frisch-Strasse D-3550 Marburg Germany Abstract Archaeoglobus fulgidus is an extremely thermophilic archaebacterium that can grow at the expense of lactate oxidation with sulfate to CO 2 and H 2 S. The organism contains coenzyme F 420 , tetrahydromethanopterin, and methanofuran which are coenzymes previously thought to be unique for methanogenic bacteria. We report here that the bacterium contains methylenetetrahydromethanopterin: F 420 oxidoreductase (20 U/mg), methenyltetrahydromethanopterin cyclohydrolase (0.9 U/mg), formyltetrahydromethanopterin: methanofuran formyltransferase (4.4 U/mg), and formylmethanofuran: benzyl viologen oxidoreductase (35 mU/mg). Besides these enzymes carbon monoxide: methyl viologen oxidoreductase (5 U/mg), pyruvate: methyl viologen oxidoreductase (0.7 U/mg), and membranebound lactate: dimethylnaphthoquinone oxidoreductase (0.1 U/mg) were found. 2-Oxoglutarate dehydrogenase, which is a key enzyme of the citric acid cycle, was not detectable. From the enzyme outfit it is concluded that in A. fulgidus lactate is oxidized to CO 2 via a modified acetyl-CoA/carbon monoxide dehydrogenase pathway involving C 1 -intermediates otherwise only used by methanogenic bacteria.

Journal

Archives of Microbiology – Springer Journals

Published: Sep 1, 1989

There are no references for this article.