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XFEL serial crystallography reveals the room temperature structure of methyl-coenzyme M reductase.
Ohmer, Christopher J; Dasgupta, Medhanjali; Patwardhan, Anjali; Bogacz, Isabel; Kaminsky, Corey; Doyle, Margaret D; Chen, Percival Yang-Ting; Keable, Stephen M; Makita, Hiroki; Simon, Philipp S; Massad, Ramzi; Fransson, Thomas; Chatterjee, Ruchira; Bhowmick, Asmit; Paley, Daniel W; Moriarty, Nigel W; Brewster, Aaron S; Gee, Leland B; Alonso-Mori, Roberto; Moss, Frank; Fuller, Franklin D; Batyuk, Alexander; Sauter, Nicholas K; Bergmann, Uwe; Drennan, Catherine L; Yachandra, Vittal K; Yano, Junko; Kern, Jan F; Ragsdale, Stephen W.
Afiliación
  • Ohmer CJ; Department of Biological Chemistry, University of Michigan Medical School, 1150 W. Medical Center Dr., 5200 MSRBIII, Ann Arbor, MI 48109-0606, USA.
  • Dasgupta M; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Patwardhan A; Department of Biological Chemistry, University of Michigan Medical School, 1150 W. Medical Center Dr., 5200 MSRBIII, Ann Arbor, MI 48109-0606, USA.
  • Bogacz I; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Kaminsky C; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Doyle MD; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Chen PY; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA.
  • Keable SM; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Makita H; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Simon PS; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Massad R; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA; Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA.
  • Fransson T; Department of Theoretical Chemistry and Biology, KTH Royal Institute of Technology, Stockholm, Sweden.
  • Chatterjee R; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Bhowmick A; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Paley DW; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Moriarty NW; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Brewster AS; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Gee LB; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
  • Alonso-Mori R; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
  • Moss F; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
  • Fuller FD; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
  • Batyuk A; LCLS, SLAC National Accelerator Laboratory, Menlo Park, CA 94025, USA.
  • Sauter NK; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Bergmann U; Department of Physics, University of Wisconsin-Madison, Madison, WI 53706, USA.
  • Drennan CL; Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; Department of Biology and the Howard Hughes Medical Institute, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA; Canadian Institute for Advanced
  • Yachandra VK; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
  • Yano J; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: jyano@lbl.gov.
  • Kern JF; Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: jfkern@lbl.gov.
  • Ragsdale SW; Department of Biological Chemistry, University of Michigan Medical School, 1150 W. Medical Center Dr., 5200 MSRBIII, Ann Arbor, MI 48109-0606, USA. Electronic address: sragsdal@umich.edu.
J Inorg Biochem ; 230: 111768, 2022 05.
Article en En | MEDLINE | ID: mdl-35202981
Methyl-Coenzyme M Reductase (MCR) catalyzes the biosynthesis of methane in methanogenic archaea, using a catalytic Ni-centered Cofactor F430 in its active site. It also catalyzes the reverse reaction, that is, the anaerobic activation and oxidation, including the cleavage of the CH bond in methane. Because methanogenesis is the major source of methane on earth, understanding the reaction mechanism of this enzyme can have massive implications in global energy balances. While recent publications have proposed a radical-based catalytic mechanism as well as novel sulfonate-based binding modes of MCR for its native substrates, the structure of the active state of MCR, as well as a complete characterization of the reaction, remain elusive. Previous attempts to structurally characterize the active MCR-Ni(I) state have been unsuccessful due to oxidation of the redox- sensitive catalytic Ni center. Further, while many cryo structures of the inactive Ni(II)-enzyme in various substrates-bound forms have been published, no room temperature structures have been reported, and the structure and mechanism of MCR under physiologically relevant conditions is not known. In this study, we report the first room temperature structure of the MCRred1-silent Ni(II) form using an X-ray Free-Electron Laser (XFEL), with simultaneous X-ray Emission Spectroscopy (XES) and X-ray Diffraction (XRD) data collection. In celebration of the seminal contributions of inorganic chemist Dick Holm to our understanding of nickel-based catalysis, we are honored to announce our findings in this special issue dedicated to this remarkable pioneer of bioinorganic chemistry.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Rayos Láser / Metano Idioma: En Revista: J Inorg Biochem Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos
Texto completo
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Rayos Láser / Metano Idioma: En Revista: J Inorg Biochem Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos