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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A90127%2F25%3A00143923" target="_blank" >RIV/00216224:90127/25:00143923 - isvavai.cz</a>

Result on the web

<a href="https://www.nature.com/articles/s41929-025-01365-y" target="_blank" >https://www.nature.com/articles/s41929-025-01365-y</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1038/s41929-025-01365-y" target="_blank" >10.1038/s41929-025-01365-y</a>

Result language

angličtina

Original language name

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

Original language description

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 &amp; 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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10611 - Plant sciences, botany

Project

—

Continuities

—

Publication year

2025

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Nature Catalysis

ISSN

2520-1158

e-ISSN

—

Volume of the periodical

8

Issue of the periodical within the volume

7

Country of publishing house

US - UNITED STATES

Number of pages

11

Pages from-to

657-667

UT code for WoS article

001527810600001

EID of the result in the Scopus database

2-s2.0-105010581003