start-ver=1.4
cd-journal=joma
no-vol=1864
cd-vols=
no-issue=2
article-no=
start-page=129466
end-page=
dt-received=
dt-revised=
dt-accepted=
dt-pub-year=2020
dt-pub=20200229
dt-online=
en-article=
kn-article=
en-subject=
kn-subject=
en-title=
kn-title=Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA
en-subtitle=
kn-subtitle=
en-abstract=
kn-abstract=Background: The invention of the X-ray free-electron laser (XFEL) has provided unprecedented new opportunities for structural biology. The advantage of XFEL is an intense pulse of X-rays and a very short pulse duration (<10 fs) promising a damage-free and time-resolved crystallography approach.<br/>
Scope of review: Recent time-resolved crystallographic analyses in XFEL facility SACLA are reviewed. Specifically, metalloproteins involved in the essential reactions of bioenergy conversion including photosystem II, cytochrome c oxidase and nitric oxide reductase are described.<br/>
Major conclusions: XFEL with pump-probe techniques successfully visualized the process of the reaction and the dynamics of a protein. Since the active center of metalloproteins is very sensitive to the X-ray radiation, damage-free structures obtained by XFEL are essential to draw mechanistic conclusions. Methods and tools for sample delivery and reaction initiation are key for successful measurement of the time-resolved data.<br/>
General significance: XFEL is at the center of approaches to gain insight into complex mechanism of structural dynamics and the reactions catalyzed by biological macromolecules. Further development has been carried out to expand the application of time-resolved X-ray crystallography. This article is part of a Special Issue entitled Novel measurement techniques for visualizing 'live' protein molecules.
en-copyright=
kn-copyright=

en-aut-name=SugaMichihiro
en-aut-sei=Suga
en-aut-mei=Michihiro
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=1
ORCID=

en-aut-name=ShimadaAtsuhiro
en-aut-sei=Shimada
en-aut-mei=Atsuhiro
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=2
ORCID=

en-aut-name=AkitaFusamichi
en-aut-sei=Akita
en-aut-mei=Fusamichi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=3
ORCID=

en-aut-name=ShenJian-Ren
en-aut-sei=Shen
en-aut-mei=Jian-Ren
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=4
ORCID=

en-aut-name=ToshaTakehiko
en-aut-sei=Tosha
en-aut-mei=Takehiko
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=5
ORCID=

en-aut-name=SugimotoHiroshi
en-aut-sei=Sugimoto
en-aut-mei=Hiroshi
kn-aut-name=
kn-aut-sei=
kn-aut-mei=
aut-affil-num=6
ORCID=

affil-num=1
en-affil=Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
kn-affil=

affil-num=2
en-affil=Graduate School of Applied Biological Sciences and Faculty of Applied Biological Sciences, Gifu University
kn-affil=

affil-num=3
en-affil=Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
kn-affil=

affil-num=4
en-affil=Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University
kn-affil=

affil-num=5
en-affil=Synchrotron Radiation Life Science Instrumentation Team, RIKEN SPring-8 Center
kn-affil=

affil-num=6
en-affil=Synchrotron Radiation Life Science Instrumentation Team, RIKEN SPring-8 Center
kn-affil=
en-keyword=Heme
kn-keyword=Heme
en-keyword=Metalloproteins
kn-keyword=Metalloproteins
en-keyword=Proton pump
kn-keyword=Proton pump
en-keyword=Radiation damage
kn-keyword=Radiation damage
en-keyword=Serial femtosecond crystallography
kn-keyword=Serial femtosecond crystallography
en-keyword=X-ray free-electron laser
kn-keyword=X-ray free-electron laser
END