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@ARTICLE{Koua:611574,
author = {Koua, Faisal Hammad Mekky and Han, Huijong and Bean,
Richard},
title = {{S}tructural {D}ynamics of {M}etalloproteins and {R}edox
{E}nzymology with {M}ix-and-{I}nject {T}ime-{R}esolved
{S}erial {F}emtosecond {C}rystallography},
journal = {ACS catalysis},
volume = {14},
number = {14},
issn = {2155-5435},
address = {Washington, DC},
publisher = {ACS},
reportid = {PUBDB-2024-04984},
pages = {10853-10870},
year = {2024},
abstract = {Time-resolved serial femtosecond crystallography (tr-SFX)
enables the study of biomolecules in action at room
temperature, thus facilitating the construction of in
crystallo mini-3D biomolecular series (a stop-motion series)
of biochemical reactions with unprecedented spatiotemporal
details. One of the challenges encountered in expanding this
method is the insufficient tools available for triggering
the biomacromolecular reaction. Here, we highlight recent
advances and challenges in the mix-and-inject
(diffusion-based) tr-SFX (MISC) as a promising triggering
method for studying the structural dynamics of
metalloproteins, redox enzymes, and their reaction kinetics.
We further discuss the results obtained using MISC tr-SFX
and propose complex MISC (cMISC) as a tool to study complex
reaction kinetics such as theenzyme-catalyzed bisubstrate
(sequential and ping-pong) reactions.},
cin = {$XFEL_E1_SPB/SFX$},
ddc = {540},
cid = {$I:(DE-H253)XFEL_E1_SPB_SFX-20210408$},
pnm = {6G13 - Accelerator of European XFEL (POF4-6G13)},
pid = {G:(DE-HGF)POF4-6G13},
experiment = {EXP:(DE-H253)XFEL-Exp-20150101},
typ = {PUB:(DE-HGF)16},
UT = {WOS:001263987000001},
doi = {10.1021/acscatal.4c02526},
url = {https://bib-pubdb1.desy.de/record/611574},
}