Thomas Gabler

Publications

24 Publications found.

• Revisiting catalytic His and Glu residues in coproporphyrin ferrochelatase - unexpected activities of active site variants

  Source: Gabler T, Dali A, Bellei M, Sebastiani F, Becucci M, Battistuzzi G, et al. Revisiting catalytic His and Glu residues in coproporphyrin ferrochelatase - unexpected activities of active site variants. The FEBS Journal. 2024;291(10):2260-72. doi:10.1111/febs.17101

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• Proximal ligand tunes active site structure and reactivity in bacterial <i>L. monocytogenes</i> coproheme ferrochelatase

  Source: A D, F S, T G, G F, DM M, DA E, et al. Proximal ligand tunes active site structure and reactivity in bacterial <i>L. monocytogenes</i> coproheme ferrochelatase. Spectrochimica acta Part a-Molecular and Biomolecular Spectroscopy. 2024;313:124120. doi:https://doi.org/10.1016/j.saa.2024.124120

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• Entrance channels to coproheme in coproporphyrin ferrochelatase probed by exogenous imidazole binding

  Source: A D, T G, F S, PG F, M B, S H, et al. Entrance channels to coproheme in coproporphyrin ferrochelatase probed by exogenous imidazole binding. Journal of Inorganic Biochemistry. 2024;260:112681. doi:10.1016/j.jinorgbio.2024.112681

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• Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III: Propionate interactions and porphyrin core deformation

  Source: A D, T G, F S, A D, PG F, V P, et al. Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III: Propionate interactions and porphyrin core deformation. Protein Science. 2023;32(1):e4534. doi:https://doi.org/10.1002/pro.4534

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• The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes.

  Source: Zámocký M, Hofbauer S, Gabler T, Furtmüller P. The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes. Biology (Basel). 2023;12(12). doi:https://doi.org/10.3390/biology12121527

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• Iron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species.

  Source: Gabler T, Dali A, Sebastiani F, Furtmüller P, Becucci M, Hofbauer S, et al. Iron insertion into coproporphyrin III-ferrochelatase complex: Evidence for an intermediate distorted catalytic species. Protein Science. 2023;32(11):e4788. doi:https://doi.org/10.1002/pro.4788

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• Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis.

  Source: Falb N, Patil G, Furtmüller P, Gabler T, Hofbauer S. Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis. Computational and Structural Biotechnology Journal. 2023;21. doi:https://doi.org/10.1016/j.csbj.2023.07.024

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• Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups.

  Source: Gabler T, Sebastiani F, Helm J, Dali A, Obinger C, Furtmüller P, et al. Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen-bonding interactions of the four propionate groups. The FEBS Journal. 2022;289(6):1680-99. doi:https://doi.org/10.1111/febs.16257

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• X-ray induced reduction of heme metal centers is protein-independent

  Source: Pfanzagl V, Beale J, Michlits H, Schmidt D, Gabler T, Obinger C, et al. X-ray induced reduction of heme metal centers is protein-independent. In: Ravy S, Thompson A , editors. 33rd European Crystallographic Meeting (ECM33). 2022.

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• Biochemistry of Enzymes Involved in the Coproporphyrin-Dependent Heme Biosynthesis Pathway of Gram-Positive Bacteria

  Source: Hofbauer S, Gabler T, Patil G, Michlits H, Pfanzagl V, Obinger C, et al. Biochemistry of Enzymes Involved in the Coproporphyrin-Dependent Heme Biosynthesis Pathway of Gram-Positive Bacteria . In: E R, A M , editors. GRC Tetrapyrroles. 2022.

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• Spectroscopic characterization of the coproporphyrin III coproporphyrin ferrochelatase complex of Listeria monocytogenes

  Source: A D, S S, T G, C O, PG F, M B, et al. Spectroscopic characterization of the coproporphyrin III coproporphyrin ferrochelatase complex of Listeria monocytogenes. In: Pogni, R , editor. OxiZymes 2022. 2022.

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• Importance of H-bonds on substrate specificity and complex stability of firmicute coproporphyrin ferrochelatase

  Source: Gabler T, Dali A, Sebastiani S, Helm J, Obinger C, Furtmüller P, et al. Importance of H-bonds on substrate specificity and complex stability of firmicute coproporphyrin ferrochelatase . In: Pogni, R , editor. OxiZymes 2022. 2022.

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• Coproporphyrin ferrochelatase – study of relevant residues for substrate and product binding

  Source: Gabler T, Pfanzagl V, Obinger C, Furtmüller PG, Hofbauer S. Coproporphyrin ferrochelatase – study of relevant residues for substrate and product binding . In: Kadish, K M , editor. ICPP-11. 2021.

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• X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner.

  Source: Pfanzagl V, Beale J, Michlits H, Schmidt D, Gabler T, Obinger C, et al. X-ray-induced photoreduction of heme metal centers rapidly induces active-site perturbations in a protein-independent manner. Journal of Biological Chemistry. 2020;295(39):13488-501. doi:https://doi.org/10.1074/jbc.RA120.014087

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• The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis.

  Source: Milazzo L, Gabler T, Pfanzagl V, Michlits H, Furtmüller P, Obinger C, et al. The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis. Journal of Inorganic Biochemistry. 2019;195:61-70. doi:https://doi.org/10.1016/j.jinorgbio.2019.03.009

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• Molecular mechanism of coproheme to heme b conversion

  Source: Hofbauer S, Milazzo L, Gabler T, Pühringer D, Pfanzagl V, Djinovic-Carugo K, et al. Molecular mechanism of coproheme to heme b conversion. In: Freisinger E, Sigel R , editors. ICBIC 19. 2019.

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• X-ray induced redcution kinetics of heme metal centers is protein-independent - implications for structural studies of redox sensitive proteins

  Source: Pfanzagl V, Beale J, Schmidt D, Michlits H, Gabler T, Djinovic-Carugo K, et al. X-ray induced redcution kinetics of heme metal centers is protein-independent - implications for structural studies of redox sensitive proteins. In: Freisinger E, Sigel R , editors. ICBIC 19. 2019.

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• X-ray induced redcution kinetics of heme metal centers is protein-independent

  Source: Pfanzagl V, Beale J, Schmidt D, Michlits H, Gabler T, Djinovic-Carugo K, et al. X-ray induced redcution kinetics of heme metal centers is protein-independent . In: Furtmüller PG, Kubala L, Obinger C , editors. HPM2019. 2019.

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• X-ray induced reduction of heme metal centers is protein-independent – implications for structural studies of redox sensitive proteins

  Source: Pfanzagl V, Beale J, Schmidt D, Michlits H, Gabler T, Djinovic-Carugo C, et al. X-ray induced reduction of heme metal centers is protein-independent – implications for structural studies of redox sensitive proteins . In: Višnjevac A, Popović J , editors. HTCC4. 2019.

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

  Source: Milazzo L, Gabler T, Pühringer D, Jandova Z, Maresch D, Michlits H, et al. Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme b. ACS Catalysis [Internet]. 2019;9:6766-82. doi:10.1021/acscatal.9b00963

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