Uwe Bergmann1,2, Jan Kern3, Robert W Schoenlein1,4, Philippe Wernet5, Vittal K Yachandra3, Junko Yano3. 1. Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, CA, USA. 2. Department of Physics, University of Wisconsin-Madison, Madison, WI, USA. 3. Molecular Biophysics and Integrated Bioimaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA. 4. Linac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA, USA. 5. Department of Physics and Astronomy, Uppsala University, Uppsala, Sweden.
Abstract
The metal centres in metalloenzymes and molecular catalysts are responsible for the rearrangement of atoms and electrons during complex chemical reactions, and they enable selective pathways of charge and spin transfer, bond breaking/making and the formation of new molecules. Mapping the electronic structural changes at the metal sites during the reactions gives a unique mechanistic insight that has been difficult to obtain to date. The development of X-ray free-electron lasers (XFELs) enables powerful new probes of electronic structure dynamics to advance our understanding of metalloenzymes. The ultrashort, intense and tunable XFEL pulses enable X-ray spectroscopic studies of metalloenzymes, molecular catalysts and chemical reactions, under functional conditions and in real time. In this Technical Review, we describe the current state of the art of X-ray spectroscopy studies at XFELs and highlight some new techniques currently under development. With more XFEL facilities starting operation and more in the planning or construction phase, new capabilities are expected, including high repetition rate, better XFEL pulse control and advanced instrumentation. For the first time, it will be possible to make real-time molecular movies of metalloenzymes and catalysts in solution, while chemical reactions are taking place.
The metal centres in n class="Chemical">metalloenzymes and molecular catalysts are responsible for the rearrangement of atoms and electrons during complex chemical reactions, and they enable selective pathways of charge and spin transfer, bond breaking/making and the formation of new molecules. Mapping the electronic structural changes at the metal sites during the reactions gives a unique mechanistic insight that has been difficult to obtain to date. The development of X-ray free-electron lasers (XFELs) enables powerful new probes of electronic structure dynamics to advance our understanding of metalloenzymes. The ultrashort, intense and tunable XFEL pulses enable X-ray spectroscopic studies of metalloenzymes, molecular catalysts and chemical reactions, under functional conditions and in real time. In this Technical Review, we describe the current state of the art of X-ray spectroscopy studies at XFELs and highlight some new techniques currently under development. With more XFEL facilities starting operation and more in the planning or construction phase, new capabilities are expected, including high repetition rate, better XFEL pulse control and advanced instrumentation. For the first time, it will be possible to make real-time molecular movies of metalloenzymes and catalysts in solution, while chemical reactions are taking place.
Authors: Yu Zhang; Thomas Kroll; Clemens Weninger; Yurina Michine; Franklin D Fuller; Diling Zhu; Roberto Alonso-Mori; Dimosthenis Sokaras; Alberto A Lutman; Aliaksei Halavanau; Claudio Pellegrini; Andrei Benediktovitch; Makina Yabashi; Ichiro Inoue; Yuichi Inubushi; Taito Osaka; Jumpei Yamada; Ganguli Babu; Devashish Salpekar; Farheen N Sayed; Pulickel M Ajayan; Jan Kern; Junko Yano; Vittal K Yachandra; Hitoki Yoneda; Nina Rohringer; Uwe Bergmann Journal: Proc Natl Acad Sci U S A Date: 2022-03-15 Impact factor: 12.779