The corrinoid-containing 23-kDa subunit MtrA of the energy-conserving N5-methyltetrahydromethanopterin:coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum. EPR spectroscopic evidence for a histidine residue as a cobalt ligand of the cobamide

European Journal of Biochemistry

Volumn 241, Issue 1, 1996, Pages 149-154

  Harms, Ulrike ^a   Thauer, Rudolf K ^a,b  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b MAX PLANCK INSTITUTE FOR TERRESTRIAL MICROBIOLOGY   (Germany)

Author keywords

Cobalamin; Corrinoids; Energy conservation; Methanogenic Archaea; Methyltransferases; Sodium ion translocaton

Indexed keywords

CORRINOID; CYTOPLASM PROTEIN; METHYLTRANSFERASE;

ARTICLE; DELETION MUTANT; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; GENE EXPRESSION; METHANOBACTERIUM THERMOAUTOTROPHICUM; METHANOGENESIS; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN FOLDING;

ARCHAEA; ESCHERICHIA COLI; METHANOBACTERIUM; METHANOTHERMOBACTER THERMAUTOTROPHICUS;

EID: 0029846834     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0149t.x     Document Type: Article

References (28)

1. Albrucht, S. P. J., Ankel-Fuchs, D., Böcher, R., Ellermann, J., Moll, J., van der Zwaan, J. W. & Thauer. R. K. (1988) Five new EPR signals assigned to nickel in methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum, strain Marburg, Biochim. Biophys. Acta 955, 86-102.
2. Becher, B., Müller, V. & Gottschalk, G. (1992) The methyl-tetrahydromethanopterin :coenzyme M methyltransferase of Methanosarcina strain Göl is a primary sodium pump, FEMS Microbiol. Lett. 91, 239-244.
3. Deppenmeier, U., Müller, V. & Gottschalk, G. (1996) Pathways of energy conservation in methanogenic archaea, Arch. Microbiol. 165, 149-163.
4. 5-Methyltetrahydromethanopterin:coenzyme M methyltransferase in methanogenic archaehacteria is a membrane protein, Arch. Microbiol. 158, 208 - 217.
5. 5-Methyltetrahydromethanopterin :coenzyme M methyltransferase from Methanobacterium thermoautotrophicum. Catalytic mechanism and sodium ion dependence. Eur. J. Biochem. 226, 465-472.
6. 5-methyltetrahydromethanopterin :coenzyme M methyltransferase from Methanobacterium thermoautotrophicum, Eur. J. Biochem. 213, 537-545.
7. 5-methyltetrahydromethanopterin :coenzyme M methyltransferase complex from Methanobacterium thermoautotrophicum is composed of eight different subunits, Eur. J. Biochem. 228, 640-648.
8. Kengen, S. W. M., Mosterd, J. J., Nelissen, R. L. H., Keltjens, J. T., van der Drift, C. & Vogels, G. D. (1988) Reductive activation of the methyl-tetrahydromethanopterin :coenzyme M methyltransferase from Methanobacterium thermoautotrophicum strain JH. Arch. Microbiol. 150, 405-412.
9. 12: the haze clears, Angew. Chem. Int. Ed. (Engl.) 35, 167 - 170.
10. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
11. Lu, W.-P., Schiau, I., Cunningham, J. R. & Ragsdale, S. W. (1993) Sequence and expression of the gene encoding the corrinoid/iron-sulfur protein from Clostridium thermoaceticum and reconstitution of the recombinant protein to full activity., J. Biol. Chem. 268, 5605-5614.
12. 12-binding domains of methionine synthase, Science 266, 1669-1674.
13. 12 radicals are generated: the crystal structure of methylmalonyl-coenzyme A mutase at 2 Å resolution, Structure 4, 339 - 350.
14. Marsh, E. N. G. & Holloway, D. E. (1992) Cloning and sequencing of glutamate mutase component S from Clostridium tetanomorpluan. Homologies with other cobalamin-dependent enzymes, FEBS Lett. 310, 167-170.
15. Maupin-Furlow, J. & Ferry, J. G. (1996) Characterization of the cdhD and cdhE genes encoding subunits of the corrinoid/iron-sulfur enzyme of the CO dehydrogenase complex from Methanosarcina thermophila, J. Bacteriol. 178, 340 - 346.
16. 12 is coordinated by histidine and not dimethylbenzimidazole on methylmalonyl-CoA mutase, J. Am. Chem. Soc. 117, 7033 - 7034.
17. 12 (Dolphin, D., ed.) pp.431 - 462, John Wiley & Sons, Inc., USA.
18. Ragsdale, S. W., Lindahl, P. A. & Münck, E. (1987) Mössbauer, EPR. and optical studies of the corrinoid/iron-sulfur protein involved in the synthesis of acetyl coenzyme A by Clostridium thermoaceticum, J. Biol. Chem. 262, 14289 - 14297.
19. Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989) Molecular cloning: a laboratory manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor NY.
20. Schmidt, F. X. (1989) Spectral methods of characterizing protein conformation and conformational changes, in Protein structure, a practical approach (Creighton, T. E., ed.) pp. 251 - 285. IRL Press, Eynsham, Oxford.
21. Schulz, H., Albracht, S. P. J., Coremans, J. M. C. C. & Fuchs, G. (1988) Purification and some properties of the corrinoid-containing membrane protein from Methanobacteriuin thermoautotrophicum, Eur. J. Biochem. 171, 589 - 597.
22. 12 in Methanobacterium thermoantotrophicum, J. Bacteriol. 169, 3076 - 3081.
23. Stupperich, E., Eisinger, H.-J. & Albracht, S. P. J. (1990) Evidence for a super-reduced cobamide as the major corrinoid fraction in vivo and a histidine residue as a cobalt ligand of the ρ-cresolyl cobamide in the acetogenic bacterium Sporomosa ovata, Eur. J. Biochem. 193, 105-109.
24. 5-methyltetrahydromethanopterin :coenzyme M methyltransferase from Methanobacterium thermoautotrophicum, Eur. J. Biochem. 217, 115-121.
25. 5-methyltetrahydromethanopterin : coenzyme M methyltransferase studied with cob(I)alamin as methyl acceptor and methylcob(III)alamin as methyl donor, Eur. J. Biochem. 226, 799 - 809.
26. Wirt, M. D., Kumar, M., Ragsdale, S. W. & Chance, M. R. (1993) X-ray absorption spectroscopy of the corrinoid/iron-sulfur protein involved in acetyl coenzyme A synthesis by Clostridium thermoaceticum, J. Am. Chem. Soc. 115, 2146 - 2150.
27. Zehnder, A. J. B. & Wuhrmann, K. (1976) Titanium(III) citrate as a nontoxic oxidation-reduction buffering system for the culture of obligate anaerobes, Science 194, 1165 - 1166.
28. 12-dependent glutamate mutase from Clostridium cochlearium, FEBS Lett. 369, 252 - 254.