Bacteria at Work - Experimental and Theoretical Studies Reveal the Catalytic Mechanism of Ectoine Synthase

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dc.contributor.authorAndrys-Olek, Justyna
dc.contributor.authorKluza, Anna
dc.contributor.authorTataruch, Mateusz
dc.contributor.authorHeider, Johann
dc.contributor.authorKorecki, Józef
dc.contributor.authorBorowski, Tomasz Maciej
dc.contributor.organizationJerzy Haber Institute of Catalysis and Surface Chemistry, Polish Academy of Sciences, Kraków, Polanden
dc.contributor.organizationDepartment of Biology, Philipps-Universität Marburg, Marburg, Germanyen
dc.date.accessioned2024-01-24T07:25:04Z
dc.date.available2024-01-24T07:25:04Z
dc.date.issued2024-01-22
dc.descriptionAuthor's Accepted Manuscripten
dc.description.abstractEctoine synthase (EctC) catalyses the ultimate step of ectoine biosynthesis, a kosmotropic compound produced as compatible solute by many bacteria and some archaea or eukaryotes. EctC is an Fe2+-dependent homodimeric cytoplasmic protein. Using Mössbauer spectroscopy, molecular dynamics simulations and QM/MM calculations, we determined the most likely coordination number and geometry of the Fe2+ ion and proposed a mechanism of the EctC-catalysed reaction. Most notably, we show that apart from the three amino acids binding to the iron ion (Glu-57, Tyr-84 and His-92), one water molecule and one hydroxide ion are required as additional ligands for the reaction to occur. They fill the first coordination sphere of the Fe2+-cofactor and act as critical proton donors and acceptors during the cyclization reaction.en
dc.description.sponsorshipThis research was funded in part by National Science Centre, Poland, grant number: UMO-2022/45/B/ST4/01411.
dc.identifier.citationChem. Eur. J. 2024, e202304163. https://doi.org/10.1002/chem.202304163en
dc.identifier.doi10.1002/chem.202304163
dc.identifier.issn1521-3765
dc.identifier.urihttps://open.icm.edu.pl/handle/123456789/23705
dc.language.isoen
dc.publisherWileyen
dc.rightsUznanie autorstwa 4.0 Międzynarodowe*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectreaction mechanismen
dc.subjectmetalloenzymeen
dc.subjectMössbauerspectroscopyen
dc.subjectQM/MMen
dc.subjectectoine synthaseen
dc.subjectironen
dc.subjectectoineen
dc.titleBacteria at Work - Experimental and Theoretical Studies Reveal the Catalytic Mechanism of Ectoine Synthaseen
dc.typearticleen
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