Light-driven hydroxylation of testosterone by Synechocystis sp. PCC 6803 expressing the heterologous CYP450 monooxygenase CYP110D1
Autor: | Francesco Mascia, Sara B. Pereira, Catarina C. Pacheco, Paulo Oliveira, Jennifer Solarczek, Anett Schallmey, Robert Kourist, Véronique Alphand, Paula Tamagnini |
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Přispěvatelé: | Institut du Cerveau = Paris Brain Institute (ICM), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Sorbonne Université (SU)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Institut de Microélectronique, Electromagnétisme et Photonique - Laboratoire d'Hyperfréquences et Caractérisation (IMEP-LAHC), Université Savoie Mont Blanc (USMB [Université de Savoie] [Université de Chambéry])-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut polytechnique de Grenoble - Grenoble Institute of Technology (Grenoble INP ), Université Grenoble Alpes (UGA), Aix Marseille Université (AMU), Instituto de Investigação e Inovação em Saúde (I3S), Universidade do Porto = University of Porto, Instituto de Biologia Molecular e Celular - institute for molecular and cell biology [Porto, Portugal] (IBMC), Institut des Sciences Moléculaires de Marseille (ISM2), Aix Marseille Université (AMU)-École Centrale de Marseille (ECM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Technische Universität Braunschweig = Technical University of Braunschweig [Braunschweig], Graz University of Technology [Graz] (TU Graz) |
Jazyk: | angličtina |
Rok vydání: | 2022 |
Předmět: | |
Zdroj: | Green Chemistry Green Chemistry, Royal Society of Chemistry, 2022, 24 (16), pp.6156-6167. ⟨10.1039/d1gc04714k⟩ Green Chemistry, 2022, 24 (16), pp.6156-6167. ⟨10.1039/d1gc04714k⟩ |
ISSN: | 1463-9262 1463-9270 |
DOI: | 10.1039/d1gc04714k⟩ |
Popis: | International audience; The selective hydroxylation of steroids through chemical synthesis is a complex reaction with a high environmental impact. The use of photoautotrophic microorganisms expressing heterologous monooxygenases could overcome this problem by fueling the reaction with electrons and O2 derived from the light-dependent oxidation of water, occurring during photosynthesis. Here, the light-driven selective hydroxylation of testosterone into 15β-hydroxytestosterone was achieved using whole-cells of the unicellular cyanobacterium Synechocystis sp. PCC 6803 expressing the heterologous CYP450 monooxygenase, CYP110D1. Additionally, the reaction conditions including cell density, aeration, and substrate concentration were optimized, leading to a maximum specific activity of 1 U gCDW−1. This value is about 2-fold higher than the one achieved using the model heterotrophic bacterium, E. coli, in which was necessary to express not only CYP110D1 but also its electron partners, and to use glucose as a sacrificial electron donor. Altogether, the results obtained here demonstrate the higher efficiency and sustainability (94% atom economy) of testosterone hydroxylation using our engineered Synechocystis chassis, compared to biocatalysis with heterotrophic microorganisms or chemical synthesis |
Databáze: | OpenAIRE |
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