MEMBRANE-BOUND F420H2-DEPENDENT HETERODISULFIDE REDUCTASE IN METHANOGENIC BACTERIUM STRAIN GOL AND METHANOLOBUS-TINDARIUS

被引：35

作者：

DEPPENMEIER, U ^{[1
]}

BLAUT, M ^{[1
]}

MAHLMANN, A ^{[1
]}

GOTTSCHALK, G ^{[1
]}

机构：

[1] UNIV GOTTINGEN,INST MIKROBIOL,GRISEBACHSTR 8,W-3400 GOTTINGEN,GERMANY

来源：

FEBS LETTERS | 1990年 / 261卷 / 01期

关键词：

F[!sub]420[!/sub; Heterodisulfide reductase; Membrane; Methane formation; Methanogenic bacteria;

D O I：

10.1016/0014-5793(90)80670-E

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Washed membrane or cytoplasmic fractions of the methanogenic bacterium strain Göl catalyzed the oxidation of coenzyme F420H2 with a variety of electron acceptors. The F420H2-oxidizing activity of the cytoplasmic fraction could be assigned to a NADP+:F420 oxidoreductase. The membrane fraction but not the cytoplasmic fraction catalyzed the oxidation of F420H2 with the concomitant reduction of the heterodisulfide of 2-mercapto-ethanesulfonate and 7-mercaptoheptanoylthreonine phosphate (CoM-S-S-HTP) at a rate of 100 nmol min-mg protein according to the following equation: F420H2+CoM-S-S-HTP → F420 + CoM + HTP-SH. The activity depended linearly on the membrane protein up to a concentration of 60 μg ml The physiological electron acceptor CoM-S-S-HTP could not be replaced by the corresponding homodisulfides CoM-S-S-CoM and HTP-S-S-HTP or by NADP+. A membrane-bound F420H2-dependent CoM-S-S-HTP reductase was also detected in Methanolobus tindarius exhibiting a specific activity of 75 nmol min m ̇g protein. The absence of a F420-dependent hydrogenase in this organism excludes the involvement of this enzyme in electron transfer from H420H2 to CoM-S-S-HTP. © 1990.

引用

页码：199 / 203

页数：5

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