Entangled hydrophobic and hydrophilic networks in carbon monoxide dehydrogenase
Year: 2026
Type: article
Abstract: /CO and water transport to the catalytic site. This likely reflects evolutionary optimization of spatially intertwined substrate access and hydration. Enhanced sampling nearly doubled enzyme hydration relative to the crystallographic model, especially near the C-clusters, while His96, Ile567, and Ser525 rearrangements govern distinct hydration pathways around the active site. Furthermore, the protonation state of His93 controls the catalytically essential water network. Our study provides an atomistic view of CODH as a finely tuned molecular nanomachine, in which entangled hydrophilic and hydrophobic networks coordinate substrate and water delivery to the C-cluster, while key protein-matrix residues act as strategic gatekeepers. Collectively, these findings reveal how dimerization, hydration, and local protein matrix cooperatively regulate critical aspects of CODH function.
Source: Chemical Science
DOI: 10.1039/d6sc04231g
Authors: Shalini Yadav, Dimitrios A. Pantazis
Institution: Max-Planck-Institut für Kohlenforschung
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: diamond
OpenAlex ID: W7204631221