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@ARTICLE{Kwiatkowski:617141,
author = {Kwiatkowski, Anna and Caserta, Giorgio and Schulz,
Anne-Christine and Frielingsdorf, Stefan and Pelmenschikov,
Vladimir and Weisser, Kilian and Belsom, Adam and
Rappsilber, Juri and Sergueev, Ilya and Limberg, Christian
and Mroginski, Maria-Andrea and Zebger, Ingo and Lenz,
Oliver},
title = {{ATP}-{T}riggered {F}e({CN})$_2${CO} {S}ynthon {T}ransfer
from the {M}aturase {H}yp{CD} to the {A}ctive {S}ite of
{A}po-[{N}i{F}e]-{H}ydrogenase},
journal = {Journal of the American Chemical Society},
volume = {146},
number = {45},
issn = {0002-7863},
address = {Washington, DC},
publisher = {ACS Publications},
reportid = {PUBDB-2024-06630},
pages = {30976-30989},
year = {2024},
note = {Additional Funding: COSTAction FeSImmChemNet, CA21115,
supported by COST(European Cooperation in Science and
Technology). The Wellcome Centre for Cell Biology is
supported by core fundingfrom the Wellcome Trust [203149]
(J.R.).},
abstract = {[NiFe]-hydrogenases catalyze the reversible activation of
H$_2$ using a unique NiFe(CN)2CO metal site, which is
assembled by a sophisticated multiprotein machinery. The
[4Fe–4S] cluster-containing HypCD complex, which possesses
an ATPase activity with a hitherto unknown function, serves
as the hub for the assembly of the Fe(CN)$_2$CO subfragment.
HypCD is also thought to be responsible for the subsequent
transfer of the iron fragment to the apo-form of the
catalytic hydrogenase subunit, but the underlying mechanism
has remained unexplored. Here, we performed a thorough
spectroscopic characterization of different HypCD
preparations using infrared, Mössbauer, and NRVS
spectroscopy, revealing molecular details of the
coordination of the Fe(CN)$_2$CO fragment. Moreover,
biochemical assays in combination with spectroscopy,
AlphaFold structure predictions, protein–ligand docking
calculations, and crosslinking MS deciphered unexpected
mechanistic aspects of the ATP requirement of HypCD, which
we found to actually trigger the transfer of the
Fe(CN)$_2$CO fragment to the apo-hydrogenase.},
cin = {DOOR ; HAS-User / FS-PET-S},
ddc = {540},
cid = {I:(DE-H253)HAS-User-20120731 /
I:(DE-H253)FS-PET-S-20190712},
pnm = {631 - Matter – Dynamics, Mechanisms and Control
(POF4-631) / 6G3 - PETRA III (DESY) (POF4-6G3) /
FS-Proposal: I-20220851 (I-20220851) / FS-Proposal:
I-20210325 (I-20210325) / DFG project G:(GEPRIS)311062227 -
Die Rolle von Eisen-Schwefel-Kofaktoren in der Assemblierung
von Metallzentren und der Katalyse von Hydrogenasen
(311062227) / DFG project G:(GEPRIS)449713269 - Design,
Synthese und Analyse von photospaltbaren chemischen
Crosslinkern zur Entwicklung von verbesserten Methoden in
der Crosslinking Massenspektrometrie (449713269) / DFG
project G:(GEPRIS)390540038 - EXC 2008: Unifying Systems in
Catalysis "UniSysCat" (390540038)},
pid = {G:(DE-HGF)POF4-631 / G:(DE-HGF)POF4-6G3 /
G:(DE-H253)I-20220851 / G:(DE-H253)I-20210325 /
G:(GEPRIS)311062227 / G:(GEPRIS)449713269 /
G:(GEPRIS)390540038},
experiment = {EXP:(DE-H253)P-P01-20150101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:39491524},
UT = {WOS:001347558800001},
doi = {10.1021/jacs.4c09791},
url = {https://bib-pubdb1.desy.de/record/617141},
}