{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T19:56:53Z","timestamp":1790798213705,"version":"4.1.0"},"reference-count":43,"publisher":"Wiley","license":[{"start":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T00:00:00Z","timestamp":1790467200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T00:00:00Z","timestamp":1790467200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22378200"],"award-info":[{"award-number":["22378200"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["22678287"],"award-info":[{"award-number":["22678287"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["advanced.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Advanced Science"],"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Integrated photo\u2010enzymatic catalysis combines the merits of both photocatalytic and enzymatic systems; however, the spatial separation of photocatalysts and enzymes in conventional one\u2010pot setups often limits overall efficiency due to sluggish electron transfer. To address this, we constructed a light\u2010driven artificial metalloenzyme (Rh\u2010L6\u2010FDH) featuring dual catalytic centers by covalently conjugating formate dehydrogenase (FDH) with a tailored rhodium complex (Rh\u2010L6), thereby facilitating synergistic NADH regeneration and CO\n                    <jats:sub>2<\/jats:sub>\n                    conversion. Screening nine synthesized Rh complexes with structurally diverse ligands revealed that Rh\u2010L6 exhibited the highest efficiency for light\u2010driven NADH regeneration. Consequently, the resulting Rh\u2010L6\u2010FDH conjugate yielded formate with a 2.31\u2010fold increase compared to the physical mixture of free FDH and Rh\u2010L6. The enhancement is mechanistically linked to the combined effects of a narrowed bandgap, diminished activation energy, and the proximity between catalytic centers, which synergistically promote charge separation and CO\n                    <jats:sub>2<\/jats:sub>\n                    activation. To overcome the inherent instability of the conjugate, Rh\u2010L6\u2010FDH was immobilized within a ZIF\u201067 framework. This strategy markedly improved catalytic robustness, boosting formate conversion to 98.4%\u2014a 16.68\u2010fold improvement over the free component system. This work demonstrates the potential of integrating molecular metal complexes with enzymes into a unified architecture, offering a promising pathway for sustainable cofactor regeneration and efficient carbon sequestration.\n                  <\/jats:p>","DOI":"10.1002\/advs.78027","type":"journal-article","created":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T18:00:31Z","timestamp":1790532031000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Engineering an Artificial Metalloenzyme for Efficient Photo\u2010Enzymatic CO\n                    <sub>2<\/sub>\n                    Conversion"],"prefix":"10.1002","author":[{"given":"Mengxue","family":"Kang","sequence":"first","affiliation":[{"name":"College of Biotechnology and Pharmaceutical Engineering State Key Laboratory of Materials\u2013Oriented Chemical Engineering Nanjing Tech University  Nanjing 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