{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kim JK"],"funding":["National Research Foundation of Korea (NRF)","Samsung","NIGMS NIH HHS"],"pagination":["4404"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12069641"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["Water plays an essential role in enzyme structure, stability, and the substantial rate enhancement of enzyme catalysis. However, direct observations linking enzyme catalysis and active-site water dynamics pose a significant challenge due to experimental difficulties. By integrating an ultraviolet (UV) photolysis technique with temperature-controlled X-ray crystallography, we track the catalytic pathway of carbonic anhydrase II (CAII) at 1.2 Å resolution. This approach enables us to construct molecular movies of CAII catalysis, encompassing substrate (CO<sub>2</sub>) binding, conversion from substrate to product (bicarbonate), and product release. In the catalytic pathway, we identify an unexpected configuration in product binding and correlate it with sub-nanosecond rearrangement of active"],"journal":["Nature communications"],"pubmed_title":["Fast product release requires active-site water dynamics in carbonic anhydrase."],"pmcid":["PMC12069641"],"funding_grant_id":["RS-2024-00353098","RS-2022-NR070463","2021R1C1C1010943","P30 GM133894","P30 GM124166","SSTF-BA1702-04","2021R1A5A8029490","2020R1C1C1003937"],"pubmed_authors":["Choi JM","Jeong H","Cohen AE","Jo BH","Kim JK","Lomelino C","Ghim CM","Wierman JL","Shin TJ","Kumar R","Kim S","Andring JT","Lee C","Son DW","Kim CU","Min D","McKenna R","Lim SW"],"additional_accession":[]},"is_claimable":false,"name":"Fast product release requires active-site water dynamics in carbonic anhydrase.","description":"Water plays an essential role in enzyme structure, stability, and the substantial rate enhancement of enzyme catalysis. However, direct observations linking enzyme catalysis and active-site water dynamics pose a significant challenge due to experimental difficulties. By integrating an ultraviolet (UV) photolysis technique with temperature-controlled X-ray crystallography, we track the catalytic pathway of carbonic anhydrase II (CAII) at 1.2 Å resolution. This approach enables us to construct molecular movies of CAII catalysis, encompassing substrate (CO<sub>2</sub>) binding, conversion from substrate to product (bicarbonate), and product release. In the catalytic pathway, we identify an unexpected configuration in product binding and correlate it with sub-nanosecond rearrangement of active","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 May","modification":"2026-06-03T02:44:56.406Z","creation":"2026-04-23T03:11:01.839Z"},"accession":"S-EPMC12069641","cross_references":{"pubmed":["40355440"],"doi":["10.1038/s41467-025-59645-x"]}}