Details
| Original language | English |
|---|---|
| Pages (from-to) | 139-148 |
| Number of pages | 10 |
| Journal | European Journal of Biochemistry |
| Volume | 220 |
| Issue number | 1 |
| Publication status | Published - Feb 1994 |
| Externally published | Yes |
Abstract
The reduction of the heterodisulfide (CoM‐S‐S‐HTP) of coenzyme M (H‐S‐CoM) and N‐7‐mercaptoheptanoylthreonine phosphate (H‐S‐HTP) with H2 is an energy‐conserving step in most methanogenic Archaea. In this study, we show that in Methanobacterium thermoautotrophicum (strain Marburg) this reaction is catalyzed by a stable H2: heterodisulfide oxidoreductase complex of F420‐non‐reducing hydrogenase and heterodisulfide reductase. This complex, which was loosely associated with the cytoplasmic membrane, was purified 17‐fold with 80% yield to apparent homogeneity. The purified complex was composed of six different subunits of apparent molecular masses 80, 51, 41, 36, 21 and 17 kDa, and 1 mol complex, with apparent molecular mass 250 kDa, contained approximately 0.6 mol nickel, 0.9 mol FAD, 26 mol non‐heme iron and 22 mol acid‐labile sulfur. In 25 nM Chaps, the complex partially dissociated into two subcomplexes. The first subcomplex was was composed of the 51‐, 41‐ and 17‐kDa subunits; 1 mol trimer contained 0.7 mol nickel, 10 mol non‐heme iron and 9 mol acid‐labile sulfur and exhibited F420‐non‐reducing hydrogenase activity. The other subcomplex was composed of the 80‐, 36‐ and 21‐kDa subunits; 1 mol trimer contained 0.8 mol FAD, 22 mol non‐heme iron and 15 mol acid‐labile sulfur and exhibited heterodisulfide‐reductase activity. The stimulatory effects of potassium phosphate, a membrane component, uracil derivatives and coenzyme F430 on the H2:heterodisulfide‐oxidoreductase activity of the purified complex are described.
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
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In: European Journal of Biochemistry, Vol. 220, No. 1, 02.1994, p. 139-148.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - H2
T2 - heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum Composition and properties
AU - Setzke, Edgar
AU - Hedderich, Reiner
AU - Heiden, Stefanie
AU - Thauer, Rudolf K.
PY - 1994/2
Y1 - 1994/2
N2 - The reduction of the heterodisulfide (CoM‐S‐S‐HTP) of coenzyme M (H‐S‐CoM) and N‐7‐mercaptoheptanoylthreonine phosphate (H‐S‐HTP) with H2 is an energy‐conserving step in most methanogenic Archaea. In this study, we show that in Methanobacterium thermoautotrophicum (strain Marburg) this reaction is catalyzed by a stable H2: heterodisulfide oxidoreductase complex of F420‐non‐reducing hydrogenase and heterodisulfide reductase. This complex, which was loosely associated with the cytoplasmic membrane, was purified 17‐fold with 80% yield to apparent homogeneity. The purified complex was composed of six different subunits of apparent molecular masses 80, 51, 41, 36, 21 and 17 kDa, and 1 mol complex, with apparent molecular mass 250 kDa, contained approximately 0.6 mol nickel, 0.9 mol FAD, 26 mol non‐heme iron and 22 mol acid‐labile sulfur. In 25 nM Chaps, the complex partially dissociated into two subcomplexes. The first subcomplex was was composed of the 51‐, 41‐ and 17‐kDa subunits; 1 mol trimer contained 0.7 mol nickel, 10 mol non‐heme iron and 9 mol acid‐labile sulfur and exhibited F420‐non‐reducing hydrogenase activity. The other subcomplex was composed of the 80‐, 36‐ and 21‐kDa subunits; 1 mol trimer contained 0.8 mol FAD, 22 mol non‐heme iron and 15 mol acid‐labile sulfur and exhibited heterodisulfide‐reductase activity. The stimulatory effects of potassium phosphate, a membrane component, uracil derivatives and coenzyme F430 on the H2:heterodisulfide‐oxidoreductase activity of the purified complex are described.
AB - The reduction of the heterodisulfide (CoM‐S‐S‐HTP) of coenzyme M (H‐S‐CoM) and N‐7‐mercaptoheptanoylthreonine phosphate (H‐S‐HTP) with H2 is an energy‐conserving step in most methanogenic Archaea. In this study, we show that in Methanobacterium thermoautotrophicum (strain Marburg) this reaction is catalyzed by a stable H2: heterodisulfide oxidoreductase complex of F420‐non‐reducing hydrogenase and heterodisulfide reductase. This complex, which was loosely associated with the cytoplasmic membrane, was purified 17‐fold with 80% yield to apparent homogeneity. The purified complex was composed of six different subunits of apparent molecular masses 80, 51, 41, 36, 21 and 17 kDa, and 1 mol complex, with apparent molecular mass 250 kDa, contained approximately 0.6 mol nickel, 0.9 mol FAD, 26 mol non‐heme iron and 22 mol acid‐labile sulfur. In 25 nM Chaps, the complex partially dissociated into two subcomplexes. The first subcomplex was was composed of the 51‐, 41‐ and 17‐kDa subunits; 1 mol trimer contained 0.7 mol nickel, 10 mol non‐heme iron and 9 mol acid‐labile sulfur and exhibited F420‐non‐reducing hydrogenase activity. The other subcomplex was composed of the 80‐, 36‐ and 21‐kDa subunits; 1 mol trimer contained 0.8 mol FAD, 22 mol non‐heme iron and 15 mol acid‐labile sulfur and exhibited heterodisulfide‐reductase activity. The stimulatory effects of potassium phosphate, a membrane component, uracil derivatives and coenzyme F430 on the H2:heterodisulfide‐oxidoreductase activity of the purified complex are described.
UR - http://www.scopus.com/inward/record.url?scp=0028177028&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1994.tb18608.x
DO - 10.1111/j.1432-1033.1994.tb18608.x
M3 - Article
C2 - 8119281
AN - SCOPUS:0028177028
VL - 220
SP - 139
EP - 148
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
SN - 0014-2956
IS - 1
ER -