Ligand binding to a Ni-Fe cluster orchestrates conformational
changes of the CO-dehydrogenase-acetyl-CoA synthase complex

J 2025

Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex

RUICKOLDT, Jakob; Julian KREIBICH; Thomas BICK; Jae-Hun JEOUNG; Benjamin R DUFFUS et al.

Základní údaje

Originální název

Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex

Autoři

RUICKOLDT, Jakob; Julian KREIBICH; Thomas BICK; Jae-Hun JEOUNG; Benjamin R DUFFUS; Silke LEIMKUEHLER; Holger DOBBEK a Petra WENDLER

Vydání

Nature Catalysis, BERLIN, Nature Portfolio, 2025, 2520-1158

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10611 Plant sciences, botany

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 44.600 v roce 2024

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90127/25:00143923

Organizační jednotka

CIISB II

Klíčová slova anglicky

CARBON-MONOXIDE DEHYDROGENASE; MULTIENZYME COMPLEX; NICKEL-COMPLEXES; MECHANISM; REVEALS; PATHWAY; METHYLBOND

Štítky

CF CRYO, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 7. 4. 2026 11:12, Mgr. Eva Dubská

Anotace

V originále

Catalytic metal clusters play critical roles in important enzymatic pathways such as carbon fixation and energy conservation. However, how ligand binding to the active-site metal regulates conformational changes critical for enzyme function is often not well understood. One carbon fixation pathway that relies heavily on metalloenzymes is the reductive acetyl-coenzyme A (acetyl-CoA) pathway. In this study, we investigated the catalysis of the last step of the reductive acetyl-CoA pathway by the CO-dehydrogenase (CODH)-acetyl-CoA synthase (ACS) complex from Carboxydothermus hydrogenoformans, focusing on how ligand binding to the nickel atom in the active site affects the conformational equilibrium of the enzyme. We captured six intermediate states of the enzyme by cryo-electron microscopy, with resolutions of 2.5-1.9 & Aring;, and visualized reaction products bound to cluster A (an Ni,Ni-[4Fe4S] cluster) and identified several previously uncharacterized conformational states of CODH-ACS. The structures demonstrate how substrate binding controls conformational changes in the ACS subunit to prepare for the next catalytic step.

Návaznosti

90242, velká výzkumná infrastruktura

Název: CIISB III

Citovat

RUICKOLDT, Jakob; Julian KREIBICH; Thomas BICK; Jae-Hun JEOUNG; Benjamin R DUFFUS; Silke LEIMKUEHLER; Holger DOBBEK a Petra WENDLER. Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex. Nature Catalysis. BERLIN: Nature Portfolio, 2025, roč. 8, č. 7, s. 657-667. ISSN 2520-1158. Dostupné z: https://doi.org/10.1038/s41929-025-01365-y.

@article{2559448,
   author = {Ruickoldt, Jakob and Kreibich, Julian and Bick, Thomas and Jeoung, JaeandHun and Duffus, Benjamin R and Leimkuehler, Silke and Dobbek, Holger and Wendler, Petra},
   article_location = {BERLIN},
   article_number = {7},
   doi = {https://doi.org/10.1038/s41929-025-01365-y},
   keywords = {CARBON-MONOXIDE DEHYDROGENASE; MULTIENZYME COMPLEX; NICKEL-COMPLEXES; MECHANISM; REVEALS; PATHWAY; METHYLBOND},
   language = {eng},
   issn = {2520-1158},
   journal = {Nature Catalysis},
   title = {Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex},
   url = {https://www.nature.com/articles/s41929-025-01365-y},
   volume = {8},
   year = {2025}
}

TY  - JOUR
ID  - 2559448
AU  - Ruickoldt, Jakob - Kreibich, Julian - Bick, Thomas - Jeoung, Jae-Hun - Duffus, Benjamin R - Leimkuehler, Silke - Dobbek, Holger - Wendler, Petra
PY  - 2025
TI  - Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex
JF  - Nature Catalysis
VL  - 8
IS  - 7
SP  - 657-667
EP  - 657-667
PB  - Nature Portfolio
SN  - 25201158
KW  - CARBON-MONOXIDE DEHYDROGENASE
KW  - MULTIENZYME COMPLEX
KW  - NICKEL-COMPLEXES
KW  - MECHANISM
KW  - REVEALS
KW  - PATHWAY
KW  - METHYLBOND
UR  - https://www.nature.com/articles/s41929-025-01365-y
N2  - Catalytic metal clusters play critical roles in important enzymatic pathways such as carbon fixation and energy conservation. However, how ligand binding to the active-site metal regulates conformational changes critical for enzyme function is often not well understood. One carbon fixation pathway that relies heavily on metalloenzymes is the reductive acetyl-coenzyme A (acetyl-CoA) pathway. In this study, we investigated the catalysis of the last step of the reductive acetyl-CoA pathway by the CO-dehydrogenase (CODH)-acetyl-CoA synthase (ACS) complex from Carboxydothermus hydrogenoformans, focusing on how ligand binding to the nickel atom in the active site affects the conformational equilibrium of the enzyme. We captured six intermediate states of the enzyme by cryo-electron microscopy, with resolutions of 2.5-1.9 & Aring;, and visualized reaction products bound to cluster A (an Ni,Ni-[4Fe4S] cluster) and identified several previously uncharacterized conformational states of CODH-ACS. The structures demonstrate how substrate binding controls conformational changes in the ACS subunit to prepare for the next catalytic step.
ER  -

RUICKOLDT, Jakob; Julian KREIBICH; Thomas BICK; Jae-Hun JEOUNG; Benjamin R DUFFUS; Silke LEIMKUEHLER; Holger DOBBEK a Petra WENDLER. Ligand binding to a Ni-Fe cluster orchestrates conformational changes of the CO-dehydrogenase-acetyl-CoA synthase complex. \textit{Nature Catalysis}. BERLIN: Nature Portfolio, 2025, roč.~8, č.~7, s.~657-667. ISSN~2520-1158. Dostupné z: https://doi.org/10.1038/s41929-025-01365-y.

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