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Reductive activation of the methyl-tetrahydromethanopterin: coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH

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Abstract

The enzymatic conversion of formaldehyde to CH3S-CoM in crude extracts of Methanobacterium thermoautotrophicum was used as a means to investigate the methyl-tetrahydromethanopterin: HS-CoM methyltransferase reaction. All components necessary for formaldehyde conversion were shown to be present in a soluble protein fraction. This soluble cell fraction still contained a major amount of corrinoids. Apart from tetrahydromethanopterin no other soluble cofactors were required for formaldehyde conversion. The dependence of the system on catalytic amounts of ATP was shown to be specific. Several nucleoside triphosphates or ADP were unable to substitute for ATP. Remarkably, various strong reducing systems, especially titanium(III)citrate could replace ATP to a large extent. The ATP-dependent formaldehyde conversion to CH3S-CoM was inhibited in the presence of nitrous oxide, detergents or 2′,3′-dialdehyde-ATP. The results support a role for a corrinoid protein in the methyl-tetrahydromethanopterin: HS-CoM methyltransferase reaction at which ATP is involved in the activation of this protein, probably in the conversion of inactive B12a or B12r to active B12s.

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Abbreviations

HS-CoM:

Coenzyme M, 2-mercaptoethanesulfonate

CH3S-CoM:

methylcoenzyme M, 2-(methylthio)ethanesulfonate

H4MPT:

5,6,7,8-tetrahydromethanopterin

BES:

2-bromoethanesulfonate

BCE:

boiled cell-free extract

DTT:

dithiothreitol

TCS:

3,3′,4,5′-tetrachlorosalicylanilide

DNTB:

2,2′-dinitro-5,5′-dithiobenzoic acid

TES:

N-tris(hydroxymethyl)methyl-2-aminoethanesulfonate

HEPES:

N-2-hydroxyethylpiperazine-N′-2-ethanesulfonic acid

PIPES:

piperazine-N,N′-bis[2-ethanesulfonic acid]

AMP-PNP:

5′-adenylyl imidophosphate

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Authors and Affiliations

  1. Department of Microbiology, Faculty of Science, University of Nijmegen, Toernooiveld, NL-6525 ED, Nijmegen, The Netherlands

    Servé W. M. Kengen, Judith J. Mosterd, Rob L. H. Nelissen, Jan T. Keltjens, Chris van der Drift & Godfried D. Vogels

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  1. Servé W. M. Kengen
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  2. Judith J. Mosterd
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  3. Rob L. H. Nelissen
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  4. Jan T. Keltjens
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  5. Chris van der Drift
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  6. Godfried D. Vogels
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Kengen, S.W.M., Mosterd, J.J., Nelissen, R.L.H. et al. Reductive activation of the methyl-tetrahydromethanopterin: coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain ΔH. Arch. Microbiol. 150, 405–412 (1988). https://doi.org/10.1007/BF00408315

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  • DOI: https://doi.org/10.1007/BF00408315

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