My Kind of Biology

Wolfe, R. S.

doi:10.1146/annurev.mi.45.100191.000245

Cited by 99 publications

(66 citation statements)

References 106 publications

(80 reference statements)

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“…We have now ruled out this possibility by showing that the methyl group of all four methylated amino acids is derived from the methyl group of methionine, most likely via S-adenosylmethionine (SAM). 1 Our experiments are based on the previous finding that methionine is taken up from the medium by growing M. thermoautotrophicum and that the methionine taken up is used for protein synthesis and in SAM-dependent methylation reactions rather than in methyl-coenzyme M-dependent methane synthesis (4). The results reported here were obtained from labeling experiments with L-[methyl-D 3 ]methionine.…”

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The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase

Selmer¹,

Kahnt²,

Goubeaud³

et al. 2000

Journal of Biological Chemistry

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The global production of the greenhouse gas methane by methanogenic archaea reaches 1 billion tons per annum. The final reaction releasing methane is catalyzed by the enzyme methyl-coenzyme M reductase. The crystal structure of methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum revealed the presence of five modified amino acids within the ␣-subunit and near the active site region. Four of these modifications were C-, N-, and S-methylations, two of which, 2-(S)-methylglutamine and 5-(S)-methylarginine, have never been encountered before. We have now confirmed these modifications by mass spectrometry of chymotryptic peptides. With methyl-coenzyme M reductase purified from cells grown in the presence of L-[methyl-D 3 ]methionine, it was shown that the methyl groups of the modified amino acids are derived from the methyl group of methionine rather than from methyl-coenzyme M, an intermediate in methane formation. The D 3 labeling pattern was found to be qualitatively and quantitatively the same as in the two methyl groups of the methanogenic coenzyme F 430 , which are known to be introduced via S-adenosylmethionine. From the results, it is concluded that the methyl groups of the modified amino acids in methyl-coenzyme M reductase are biosynthetically introduced by an S-adenosylmethioninedependent post-translational modification. A mechanism for the methylation of glutamine at C-2 and of arginine at C-5 is discussed.Methyl-coenzyme M reductase catalyzes the final reaction step in the formation of methane by methanogenic archaea. It is a 300-kDa protein composed of three different subunits in an ␣ 2 ␤ 2 ␥ 2 arrangement and contains per mol 2 mol of the nickel porphinoid coenzyme F 430 as prosthetic group (1, 2). The crystal structure of the enzyme from Methanobacterium thermoautotrophicum has recently been solved at 1.45-Å resolution (3). The electron density map suggested the presence of five modified amino acids in the ␣ subunits either at or very near the active site region: 1-N-methylhistidine ␣257 (3-methylhistidine according to IUPAC nomenclature), 5-(S)-methylarginine ␣271, 2-(S)-methylglutamine ␣400, S-methylcysteine ␣452, and thioglycine ␣445, forming a thiopeptide bond (Fig. 1). Thioglycine has been proposed to function as a one-electron relay in the catalytic mechanism (2). Methylation of histidine ␣257, which is involved in substrate binding, probably influences the substrate affinity of the enzyme (3). For the methylation of the three other amino acids, an accidental methylation via methylcoenzyme M-derived methyl radicals has been envisaged. We have now ruled out this possibility by showing that the methyl group of all four methylated amino acids is derived from the methyl group of methionine, most likely via S-adenosylmethionine (SAM).1 Our experiments are based on the previous finding that methionine is taken up from the medium by growing M. thermoautotrophicum and that the methionine taken up is used for protein synthesis and in SAM-dependent methylation reactions rather than in met...

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“…It is a 300-kDa protein composed of three different subunits in an ␣ 2 ␤ 2 ␥ 2 arrangement and contains per mol 2 mol of the nickel porphinoid coenzyme F 430 as prosthetic group (1,2). The crystal structure of the enzyme from Methanobacterium thermoautotrophicum has recently been solved at 1.45-Å resolution (3).…”

mentioning

confidence: 99%

The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase

Selmer¹,

Kahnt²,

Goubeaud³

et al. 2000

Journal of Biological Chemistry

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“…With the anaplerotic reaction found by Lie et al (3), the cycle of CO 2 reduction to methane is finally complete. This methanogenic cycle is now referred to as the Wolfe cycle, in honor of Ralph S. Wolfe (22), who has been the motor driving its elucidation.…”

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The Wolfe cycle comes full circle

Thauer

2012

Proc. Natl. Acad. Sci. U.S.A.

108

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“…For detailed information on the reactions, enzymes and coenzymes involved in methanogenesis from CO, and H, the reader is referred to recent reviews by DiMarco et al (1990), Wolfe (1991), Weiss and Thauer (1993) and Thauer et al (1993).…”

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confidence: 99%

H₂: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum

Setzke

Hedderich

Heiden

et al. 1994

European Journal of Biochemistry

100

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The reduction of the heterodisulfide (CoM-S-S-HTP) of coenzyme M (H-S-CoM) and N-7-mercaptoheptanoylthreonine phosphate (H-S-HTP) with H, 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 H, :heterodisulfide oxidoreductase complex of F4,,,-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 mM 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 F,,,-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 F,,, on the H, :heterodisulfide-oxidoreductase activity of the purified complex are described.

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My Kind of Biology

Cited by 99 publications

References 106 publications

The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase

The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase

The Wolfe cycle comes full circle

H₂: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum

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My Kind of Biology

Cited by 99 publications

References 106 publications

The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase

The Biosynthesis of Methylated Amino Acids in the Active Site Region of Methyl-coenzyme M Reductase

The Wolfe cycle comes full circle

H2: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum

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H₂: heterodisulfide oxidoreductase complex from Methanobacterium thermoautotrophicum