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Milazzo L, Gabler T, Pühringer D, et al. Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme . ACS Catal. 2019;9(8):6766-6782doi: 10.1021/acscatal.9b00963.
Milazzo, L., Gabler, T., Pühringer, D., Jandova, Z., Maresch, D., Michlits, H., Pfanzagl, V., Djinović-Carugo, K., Oostenbrink, C., Furtmüller, P. G., Obinger, C., Smulevich, G., & Hofbauer, S. (2019). Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme . ACS catalysis, 9(8), 6766-6782. https://doi.org/10.1021/acscatal.9b00963
Milazzo, Lisa, et al. "Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme ." ACS catalysis vol. 9,8 (2019): 6766-6782. doi: https://doi.org/10.1021/acscatal.9b00963
Milazzo L, Gabler T, Pühringer D, Jandova Z, Maresch D, Michlits H, Pfanzagl V, Djinović-Carugo K, Oostenbrink C, Furtmüller PG, Obinger C, Smulevich G, Hofbauer S. Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme . ACS Catal. 2019 Aug 02;9(8):6766-6782. doi: 10.1021/acscatal.9b00963. Epub 2019 Jun 18. PMID: 31423350; PMCID: PMC6691569.
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ACS Catal. 2019 Aug 02;9(8):6766-6782. doi: 10.1021/acscatal.9b00963. Epub 2019 Jun 18.

Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme .

ACS catalysis

Lisa Milazzo, Thomas Gabler, Dominic Pühringer, Zuzana Jandova, Daniel Maresch, Hanna Michlits, Vera Pfanzagl, Kristina Djinović-Carugo, Chris Oostenbrink, Paul G Furtmüller, Christian Obinger, Giulietta Smulevich, Stefan Hofbauer

Affiliations

  1. Dipartimento di Chimica "Ugo Schiff", Università di Firenze, Via della Lastruccia 3-13, I-50019 Sesto Fiorentino (FI), Italy.
  2. Department of Chemistry, Division of Biochemistry, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
  3. Department for Structural and Computational Biology, Max F. Perutz Laboratories, University of Vienna, A-1030 Vienna, Austria.
  4. Department of Material Sciences and Process Engineering, Institute of Molecular Modeling and Simulation, BOKU-University of Natural Resources and Life Sciences, A-1190 Vienna, Austria.
  5. Department of Biochemistry, Faculty of Chemistry and Chemical Technology, University of Ljubljana, 1000 Ljubljana, Slovenia.

PMID: 31423350 PMCID: PMC6691569 DOI: 10.1021/acscatal.9b00963

Abstract

Coproheme decarboxylase (ChdC) catalyzes the last step in the heme biosynthesis pathway of monoderm bacteria with coproheme acting both as redox cofactor and substrate. Hydrogen peroxide mediates the stepwise decarboxylation of propionates 2 and 4 of coproheme. Here we present the crystal structures of coproheme-loaded ChdC from

Conflict of interest statement

The authors declare no competing financial interest.

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