An algal photoenzyme converts fatty acids to hydrocarbons

Author:

Sorigué Damien1ORCID,Légeret Bertrand1ORCID,Cuiné Stéphan1ORCID,Blangy Stéphanie1ORCID,Moulin Solène1ORCID,Billon Emmanuelle1ORCID,Richaud Pierre1,Brugière Sabine2,Couté Yohann2ORCID,Nurizzo Didier3ORCID,Müller Pavel4ORCID,Brettel Klaus4ORCID,Pignol David5,Arnoux Pascal5ORCID,Li-Beisson Yonghua1ORCID,Peltier Gilles1ORCID,Beisson Fred1ORCID

Affiliation:

1. Biosciences and Biotechnologies Institute of Aix-Marseille (BIAM), Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), CNRS and Aix-Marseille University, UMR 7265 LB3M, CEA Cadarache, F-13108, Saint-Paul-lez-Durance, France.

2. University Grenoble Alpes, CEA and INSERM, BIG-BGE, F-38000, Grenoble, France.

3. European Synchrotron Radiation Facility, 71 Avenue des Martyrs, CS 40220, F-38043 Grenoble, France.

4. Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, University Paris-Sud, University Paris-Saclay, F-91198, Gif-sur-Yvette cedex, France.

5. BIAM, CEA, CNRS and Aix-Marseille University, UMR 7265 LBC, CEA Cadarache, F-13108, Saint-Paul-lez-Durance, France.

Abstract

Algal enzyme driven by blue light Microalgae make hydrocarbons. In searching for the enzyme responsible, Sorigué et al. found a glucose-methanolcholine oxidoreductase (see the Perspective by Scrutton). Expression of the enzyme in Escherichia coli showed that hydrocarbon production requires visible light. In fact, the enzyme requires a constant input of blue photons to carry out its catalytic reaction. A long hydrophobic tunnel in the enzyme stabilizes the fatty acid substrates in proximity to the flavin adenine dinucleotide cofactor. Science , this issue p. 903 ; see also p. 872

Funder

Agence Nationale de la Recherche

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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