On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.

@article{Grabarse2001OnTM,
  title={On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding.},
  author={Wolfgang Grabarse and Felix Mahlert and Evert C. Duin and M Goubeaud and Seigo Shima and Rudolf Kurt Thauer and Victor S. Lamzin and Ulrich Ermler},
  journal={Journal of molecular biology},
  year={2001},
  volume={309 1},
  pages={315-30}
}
Methyl-coenzyme M reductase (MCR) catalyzes the final reaction of the energy conserving pathway of methanogenic archaea in which methylcoenzyme M and coenzyme B are converted to methane and the heterodisulfide CoM-S-S-CoB. It operates under strictly anaerobic conditions and contains the nickel porphinoid F430 which is present in the nickel (I) oxidation state in the active enzyme. The known crystal structures of the inactive nickel (II) enzyme in complex with coenzyme M and coenzyme B (MCR-ox1… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 14 extracted citations

Similar Papers

Loading similar papers…