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PreprintCited by 2Microbial Metabolic Engineering and BioproductionPhotosynthetic Processes and MechanismsEnzyme Catalysis and Immobilization

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Harnessing photosynthetic ATP for whole-cell biocatalysis in the cyanobacterium Synechocystis

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Loprete, Giovanni, Traverso, Eleonora, Vascon, Filippo, Botteri, Marco, Robescu, Marina Simona, Ubiali, Daniela, Cendron, Laura, Morosinotto, Tomas, Bergantino, Elisabetta·2025·ACS Sustainable Chemistry & Engineering
DOI 10.1101/2025.05.29.656799PMC PMC12588301

Preprint — published as 10.1021/acssuschemeng.5c07236 · Paper page

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Abstract

Photosynthetic organisms use sunlight to produce ATP and NADPH powering their metabolism. Harnessing these products for driving biocatalytic reactions would enable to develop clean and sustainable alternatives for chemical reactions. In this study, we present the first demonstration that ATP produced from the photosynthetic process, can fuel a biocatalytic transformation in the whole-cell configuration. This result was achieved by expressing in the cyanobacterium Synechocystis sp. PCC 6803 an ATP-dependent enzyme, the γ-Glutamyl-MethylAmide Synthetase from Methylovorus mays No. 9 ( Mm GMAS). The expressed enzyme was able to drive in the transgenic strain the light-driven biosynthesis of L-theanine. Consumption of ATP by the recombinant Mm GMAS was even beneficial under strong illumination, protecting the photosynthetic electron transport from photodamage. These findings demonstrate the possibility of using photosynthetic microorganisms like Synechocystis as potential platform for sunlight driven biotransformations with wide potential biocatalytic applications. In this perspective, we further present the tridimensional structure of Mm GMAS, which explains its promiscuous in vivo activity and provides the basis for its rational evolution.

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Metadata

Authors
Loprete, G., Traverso, E., Vascon, F., Botteri, M., Robescu, M. S., Ubiali, D., Cendron, L., Morosinotto, T., & Bergantino, E.
Affiliations
  • University of Padua (IT)
  • University of Pavia (IT)
Corresponding author
Bergantino, Elisabetta
ORCID
Venue
ACS Sustainable Chemistry & Engineering
Publisher
openRxiv
Published
2025-05-30
Volume
13
Issue
43
Pages
18667-18677
ISSN
2168-0485 (ISSN-L)
DOI
10.1101/2025.05.29.656799
PMC
PMC12588301
OpenAlex
W4415468576
Cited by
2
References
2
Citations by year
2026: 2
FWCI
0.60
Type
journal article
Language
en
Open access
Licence
Locations
  • ACS Sustainable Chemistry & Engineering (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Padua Research Archive (University of Padova) (submittedVersion, cc-by)
Funders
  • European Commission (ECS_00000036)
  • European Synchrotron Radiation Facility (ID30A-3)
  • Università degli Studi di Padova
  • Dipartimento di Biologia, Università degli Studi di Padova (BIRD221528/22, U-GOV CEND_BIRD24_01)
  • NextGenerationEU (ECS00000036)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
Keywords
whole-cell biocatalysis, Synechocystis sp. PCC 6803, ATP-dependent enzyme, enzyme structure, cyanobacteria

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