The pH-induced selectivity between cysteine or histidine coordinated heme in an artificial α-helical metalloprotein

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dc.contributor.authorKoebke, Karl J.
dc.contributor.authorKühl, Toni
dc.contributor.authorLojou, Elisabeth
dc.contributor.authorDemeler, Borries
dc.contributor.authorSchoepp-Cothenet, Barbara
dc.contributor.authorIranzo, Olga
dc.contributor.authorPecoraro, Vincent L.
dc.contributor.authorIvancich, Anabella
dc.date.accessioned2022-10-25T16:49:12Z
dc.date.available2022-10-25T16:49:12Z
dc.date.issued2021
dc.descriptionAccepted author manuscripten_US
dc.description.abstractDe Novo metalloprotein design assesses the relationship between metal active site architecture and catalytic reactivity. Herein, we use an α-helical scaffold to control the iron coordination geometry when a heme cofactor is allowed to bind to either histidine or cysteine ligands, within a single artificial protein. Consequently, we uncovered a reversible pH-induced switch of the heme axial ligation within this simplified scaffold. Characterization of the specific heme coordination modes was done by using UV-Vis and Electron Paramagnetic Resonance spectroscopies. The penta- or hexa-coordinate thiolate heme (9 ≤ pH ≤ 11) and the penta-coordinate imidazole heme (6 ≤ pH ≤ 8.5) reproduces well the heme ligation in chloroperoxidases or cyt P450 monooxygenases and peroxidases, respectively. The stability of heme coordination upon ferric/ferrous redox cycling is a crucial property of the construct. At basic pHs, the thiolate mini-heme protein can catalyze O2 reduction when adsorbed onto a pyrolytic graphite electrode.en_US
dc.description.peer-reviewYesen_US
dc.identifier.citationKoebke, K. J., Kühl, T., Lojou, E., Demeler, B., Schoepp-Cothenet, B., Iranzo, O., Pecoraro, V. L., & Ivancich, A. (2021). The pH-induced selectivity between cysteine or histidine coordinated heme in an artificial α-helical metalloprotein. Angewandte Chemie International Edition, 2021, 60(8), 3974-3978. https://doi.org/10.1002/anie.202012673en_US
dc.identifier.urihttps://hdl.handle.net/10133/6359
dc.language.isoen_USen_US
dc.publisherWileyen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionUniversity of Michiganen_US
dc.publisher.institutionAix-Marseille Universityen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://doi.org/10.1002/anie.202012673en_US
dc.subjectDe Novo protein designen_US
dc.subjectCyt P450 monooxygenaseen_US
dc.subjectHeme enzymesen_US
dc.subjectThiolate ligandsen_US
dc.subjectEPR spectroscopyen_US
dc.subject.lcshProtein engineering
dc.subject.lcshMonooxygenases
dc.subject.lcshCytochrome P-450
dc.subject.lcshThiolates
dc.subject.lcshElectron paramagnetic resonance spectroscopy
dc.titleThe pH-induced selectivity between cysteine or histidine coordinated heme in an artificial α-helical metalloproteinen_US
dc.typeArticleen_US
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