TY  - JOUR
AU  - Kwiatkowski, Anna
AU  - Caserta, Giorgio
AU  - Schulz, Anne-Christine
AU  - Frielingsdorf, Stefan
AU  - Pelmenschikov, Vladimir
AU  - Weisser, Kilian
AU  - Belsom, Adam
AU  - Rappsilber, Juri
AU  - Sergueev, Ilya
AU  - Limberg, Christian
AU  - Mroginski, Maria-Andrea
AU  - Zebger, Ingo
AU  - Lenz, Oliver
TI  - ATP-Triggered Fe(CN)<sub>2</sub>CO Synthon Transfer from the Maturase HypCD to the Active Site of Apo-[NiFe]-Hydrogenase
JO  - Journal of the American Chemical Society
VL  - 146
IS  - 45
SN  - 0002-7863
CY  - Washington, DC
PB  - ACS Publications
M1  - PUBDB-2024-06630
SP  - 30976-30989
PY  - 2024
N1  - 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.).
AB  - [NiFe]-hydrogenases catalyze the reversible activation of H<sub>2</sub> 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)<sub>2</sub>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)<sub>2</sub>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)<sub>2</sub>CO fragment to the apo-hydrogenase.
LB  - PUB:(DE-HGF)16
C6  - pmid:39491524
UR  - <Go to ISI:>//WOS:001347558800001
DO  - DOI:10.1021/jacs.4c09791
UR  - https://bib-pubdb1.desy.de/record/617141
ER  -