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PMID: 9546664 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from the hyperthermophilic Pyrodictium abyssi.

European journal of biochemistry ·Vol. 252 ·No. 3 ·1998-03-15 ·Pages 486-91

Dirmeier R, Keller M, Frey G, Huber H, Stetter KO

Abstract

The chemolithoautotrophic archaeon Pyrodictium abyssi isolate TAG 11 gains energy by reducing sulfur with H2 to H2S. From this hyperthermophile, a sulfur-reducing complex catalyzing this reaction was purified 13.5-fold. The native complex exhibited a brownish-yellow colour and showed an apparent molecular mass of 520 kDa. SDS/PAGE revealed the presence of nine different major polypeptides with apparent molecular masses of 82, 72, 65, 50, 47, 42, 40, 30 and 24 kDa. The native complex contained 50-55 mol acid-labile sulfur, 50-55 mol iron, 1.6 mol nickel, 1.2 mol copper, 2.8 mol cytochrome b and 0.3 mol cytochrome c (all per mol native complex). The temperature optimum of the H2:sulfur oxidoreductase complex was 100 degrees C, which is consistent with the physiological growth optimum of the native organism. The complex is extremely heat stable. During 5 h incubation at 100 degrees C, no decrease in H2S-forming activity could be observed.

MeSH Terms
Amino Acid Sequence Archaea/enzymology Bacteria/enzymology Cell Membrane/enzymology Chromatography, Gel Cytochrome b Group/metabolism Cytochrome c Group/metabolism Desulfurococcaceae/enzymology,growth & development Hot Temperature Kinetics Macromolecular Substances Molecular Sequence Data Molecular Weight Multienzyme Complexes/chemistry,isolation & purification,metabolism Oxidation-Reduction Oxidoreductases/chemistry,isolation & purification,metabolism Sequence Alignment Sequence Homology, Amino Acid Sulfur/metabolism
Chemicals
Cytochrome b Group Cytochrome c Group Macromolecular Substances Multienzyme Complexes Sulfur Oxidoreductases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Dirmeier R
Lehrstuhl für Mikrobiologie, Regensburg, Germany. reinhard.dirmeier@biologie.uni-regensburg.de
Keller M
Frey G
Huber H
Stetter K O
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1998-03-15
Pages
486-91
Language
English
Region
England
NLM ID
0107600
Subset
IM
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