{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,15]],"date-time":"2026-09-15T15:51:26Z","timestamp":1789487486537,"version":"build-2803163510"},"reference-count":49,"publisher":"American Chemical Society (ACS)","issue":"36","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,9,15]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>In this work, the design of CYP116B5-SOX(PPII) is presented. This is an artificial self-sufficient enzyme in which the P450 116B5 peroxygenase and the H2O2-generating sarcosine oxidase (SOX) are linked together in a fusion complex. A polyproline type II helix (PPII) linker was used to connect the two enzymes, obtaining a rigid fusion protein. CYP116B5-SOX(PPII) displayed 10-fold increased activity in terms of p-nitrophenol oxidation (kcat: 32.1 \u00b1 0.5 min\u20131; KM: 150 \u00b1 15 \u03bcM) compared to the isolated heme domain CYP116B5-hd, and more than 2-fold higher activity compared to CYP116B5-SOX\u2500a fusion enzyme in which the two domains are passively linked by a flexible polyglycine sequence. The stability of the three CYP116B5 variants was investigated by differential scanning calorimetry. The data revealed the higher folding cooperativity of the P450 domain within the rigid fusion system, as well as the stabilization of the SOX domain compared to CYP116B5-SOX. The catalytic stability of the fusion enzymes was confirmed by testing the single domains\u2019 residual activity after thermal denaturation. The interdomain plasticity of the two fusion enzymes was analyzed by H\/D exchange kinetics experiments through ATR-FTIR spectroscopy. The results revealed that the flexible CYP116B5-SOX exhibits a globally lower protein surface accessibility to water compared to the rigid CYP116B5-SOX(PPII), suggesting that the formation of interdomain contacts is disadvantageous for this fusion couple. CYP116B5 shows some activity toward styrene oxidation into styrene oxide and phenylacetaldehyde (KM: 9.0 \u00b1 2.9 mM, kcat: 1.9 \u00b1 0.3 min\u20131). Interestingly, E. coli cells expressing CYP116B5-SOX(PPII) show 56% styrene conversion when hydrogen peroxide is produced in situ by SOX, whereas only 13% conversion is reached when hydrogen peroxide is directly added in solution. Overall, this work shows that the stability and catalytic efficiency of the artificial chimera are intimately associated with the quaternary assembly of the construct, unveiling the crucial role of the fusion design for the extensive exploitation of P450 biocatalysis.<\/jats:p>","DOI":"10.1021\/acsomega.6c07054","type":"journal-article","created":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T14:16:08Z","timestamp":1788444968000},"page":"54593-54602","source":"Crossref","is-referenced-by-count":0,"title":["Effect of Linker\nSequence on the Interdomain Dynamics\nof Self-Sufficient CYP116B5-SOX Chimeras"],"prefix":"10.1021","volume":"11","author":[{"given":"Daniele","family":"Giuriato","sequence":"first","affiliation":[{"name":"University of Torino , , via Accademia Albertina 13 , ,","place":["Torino, Italy, 10123"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lorenzo","family":"Gorga","sequence":"additional","affiliation":[{"name":"University of Torino , , via Accademia Albertina 13 , ,","place":["Torino, Italy, 10123"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Silvia","family":"Castrignano\u0300","sequence":"additional","affiliation":[{"name":"University of Torino , , via Accademia Albertina 13 , ,","place":["Torino, Italy, 10123"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Danilo","family":"Correddu","sequence":"additional","affiliation":[{"name":"University of Torino , , via Accademia Albertina 13 , ,","place":["Torino, Italy, 10123"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gianluca","family":"Catucci","sequence":"additional","affiliation":[{"name":"University of Torino , , via Accademia Albertina 13 , ,","place":["Torino, Italy, 10123"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-6559-276X","authenticated-orcid":true,"given":"Gianfranco","family":"Gilardi","sequence":"additional","affiliation":[{"name":"University of Torino , , via Accademia Albertina 13 , ,","place":["Torino, Italy, 10123"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,1]]},"reference":[{"key":"2026091510075745100_cit1","doi-asserted-by":"publisher","first-page":"108016","DOI":"10.1016\/j.biotechadv.2022.108016","article-title":"Design and Biocatalytic\nApplications\nof Genetically Fused Multifunctional Enzymes","volume":"60","author":"Monterrey","year":"2022","journal-title":"Biotechnol. 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Mol. Catal.\nB: Enzym."},{"issue":"50","key":"2026091510075745100_cit33","doi-asserted-by":"publisher","first-page":"14771","DOI":"10.1021\/bi026383q","article-title":"Structure and Dynamics of the Modular\nHalves of Escherichia Coli Cyclic AMP\nReceptor Protein","volume":"41","author":"Li","year":"2002","journal-title":"Biochemistry"},{"issue":"8","key":"2026091510075745100_cit34","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1111\/j.1745-7270.2007.00320.x","article-title":"Fourier Transform Infrared\nSpectroscopic Analysis of Protein Secondary\nStructures","volume":"39","author":"Kong","year":"2007","journal-title":"ABBS"},{"key":"2026091510075745100_cit35","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1146\/annurev.biophys.29.1.213","article-title":"Protein\nFolding Intermediates and Pathways Studied by Hydrogen Exchange","volume":"29","author":"Englander","year":"2000","journal-title":"Annu. Rev. 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A."},{"key":"2026091510075745100_cit43","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1016\/bs.mie.2020.09.012","article-title":"Predicting\nthe Effect of Disordered\nLinkers on Effective Concentrations and Avidity with the \u201cCEff\nCalculator\u201d App","volume":"647","author":"Kjaergaard","year":"2021","journal-title":"Methods Enzymol."},{"key":"2026091510075745100_cit44","doi-asserted-by":"publisher","first-page":"1484","DOI":"10.1016\/j.ijbiomac.2020.08.032","article-title":"Ligand Stabilization\nand Effect on Unfolding by Polymorphism in Human Flavin-Containing\nMonooxygenase 3","volume":"162","author":"Catucci","year":"2020","journal-title":"Int. J. Biol. Macromol."},{"issue":"16","key":"2026091510075745100_cit45","doi-asserted-by":"publisher","first-page":"2443","DOI":"10.1002\/cbic.201402309","article-title":"Unusually\nBroad Substrate Profile of Self-Sufficient\nCytochrome P450 Monooxygenase CYP116B4 from Labrenzia Aggregata","volume":"15","author":"Yin","year":"2014","journal-title":"ChemBioChem"},{"issue":"1","key":"2026091510075745100_cit46","doi-asserted-by":"publisher","first-page":"140268","DOI":"10.1016\/j.bbapap.2019.140268","article-title":"Expression\nand role of CYP505A1 in pathogenicity of Fusarium oxysporum f. sp.\nlactucae","volume":"1868","author":"Minerdi","year":"2020","journal-title":"Biochim. Biophys. 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