Activation of formylmethanofuran synthesis in cell extracts of Methanobacterium thermoautotrophicum

Author:

Bobik T A1,Wolfe R S1

Affiliation:

1. Department of Microbiology, University of Illinois, Urbana 61801.

Abstract

In cell extracts of Methanobacterium thermoautotrophicum, formylmethanofuran (formyl-MFR) synthesis (an essential CO2 fixation reaction that is an early step in CO2 reduction to methane) is subject to a complex activation that involves a heterodisulfide of coenzyme M and N-(7-mercaptoheptanoyl)threonine O3-phosphate (CoM-S-S-HTP). In this paper we report that titanium(III) citrate, a low-potential reducing agent, stimulated CO2 reduction to methane and activated formyl-MFR synthesis in cell extracts. Titanium(III) citrate functioned as the sole source of electrons for formyl-MFR synthesis and enabled this reaction to occur independently of CoM-S-S-HTP. In addition, CoM-S-S-HTP was found to activate an unknown electron carrier that reduced metronidazole. The activation of formyl-MFR synthesis by CoM-S-S-HTP may involve the activation of a low-potential electron carrier.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference30 articles.

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2. Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium;Bobik T. A.;Biochem. Biophys. Res. Commun.,1987

3. Physiological importance of the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate in the reduction of carbon dioxide to methane in Methanobacterium;Bobik T. A.;Proc. Natl. Acad. Sci. USA,1988

4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding;Bradford M. M.;Anal. Biochem.,1976

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