@article{1059d54e664d4962848d6840d228825e,
title = "Snapshot of an oxygen intermediate in the catalytic reaction of cytochrome c oxidase",
abstract = " Cytochrome c oxidase (CcO) reduces dioxygen to water and harnesses the chemical energy to drive proton translocation across the inner mitochondrial membrane by an unresolved mechanism. By using time-resolved serial femtosecond crystallography, we identified a key oxygen intermediate of bovine CcO. It is assigned to the P R -intermediate, which is characterized by specific redox states of the metal centers and a distinct protein conformation. The heme a 3 iron atom is in a ferryl (Fe 4+ = O 2− ) configuration, and heme a and Cu B are oxidized while Cu A is reduced. A Helix-X segment is poised in an open conformational state; the heme a farnesyl sidechain is H-bonded to S382, and loop-I-II adopts a distinct structure. These data offer insights into the mechanism by which the oxygen chemistry is coupled to unidirectional proton translocation.",
keywords = "Bioenergetics, Catalytic intermediates, Complex IV, Crystallography, X-ray free electron laser",
author = "Izumi Ishigami and Ariel Lewis-Ballester and Austin Echelmeier and Gerrit Brehm and Zatsepin, {Nadia A.} and Grant, {Thomas D.} and Coe, {Jesse D.} and Stella Lisova and Garrett Nelson and Shangji Zhang and Dobson, {Zachary F.} and S{\'e}bastien Boutet and Sierra, {Raymond G.} and Alexander Batyuk and Petra Fromme and Raimund Fromme and Spence, {John C.H.} and Alexandra Ros and Yeh, {Syun Ru} and Rousseau, {Denis L.}",
note = "Funding Information: The SFX experiments were carried out at the Macromolecular Femtosecond Crystallography experimental station at the Linac Coherent Light Source (LCLS) at the SLAC National Accelerator Laboratory. LCLS is an Office of Science User Facility operated for the US Department of Energy Office of Science by Stanford University. Use of the LCLS, SLAC National Accelerator Laboratory, is supported by the US Department of Energy, Office of Science and Office of Basic Energy Sciences under Contract DE-AC02-76SF00515. The helium-rich ambient system for in helium experiments at Macromolecular Femtosecond Crystallography was developed by Bruce Doak and funded by the Max Planck Institute for Medical Research. This work was supported by National Science Foundation Science and Technology Centers Award 1231306, CHE-1404929 (to D.L.R. and S.-R.Y.); Directorate for Biological Sciences Advances in Biological Informatics Grant 1565180 (to N.A.Z. and J.C.H.S.); and National Institutes of Health Awards GM098799 and GM126297 (to D.L.R. and S.-R.Y.) and GM115773 (to S.-R.Y.), and R01GM095583 (to P.F. and A.R.). We also acknowledge support from the Biodesign Center for Applied Structural Discovery at Arizona State University. Publisher Copyright: {\textcopyright} 2019 National Academy of Sciences. All Rights Reserved.",
year = "2019",
month = feb,
day = "26",
doi = "10.1073/pnas.1814526116",
language = "English (US)",
volume = "116",
pages = "3572--3577",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "National Academy of Sciences",
number = "9",
}