Daniel Schmidt

Publications

14 Publications found.

• Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine.

  Source: Schmidt D, Falb N, Serra I, Bellei M, Pfanzagl V, Hofbauer S, et al. Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine. Biochemistry. 2023;62(3):83-850. doi:https://doi.org/10.1021/acs.biochem.2c00696

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• Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase.

  Source: Serra I, Schmidt D, Pfanzagl V, Mlynek G, Hofbauer S, Djinović-Carugo K, et al. Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase. Journal of Inorganic Biochemistry. 2022;227:111689. doi:https://doi.org/10.1016/j.jinorgbio.2021.111689

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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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• Structural and mechanistic insights in dimeric chlorite dismutase - Impact of pH and the dynamics of the catalytic arginine

  Source: Schmidt D, Serra I, Hofbauer S, Pfanzagl V, Van Doorslaer S, Obinger C, et al. Structural and mechanistic insights in dimeric chlorite dismutase - Impact of pH and the dynamics of the catalytic arginine . In: Duboc, C , editor. 16th European Biological Inorganic Chemistry [Internet]. 2022. Available from: https://eurobic16.sciencesconf.org/

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  eurobic16.sciencesconf.org

• Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions.

  Source: Hofbauer S, Pfanzagl V, Michlits H, Schmidt D, Obinger C, Furtmüller P. Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions. Biochimica Et Biophysica acta-Proteins and Proteomics. 2021;1869(1):140536. doi:https://doi.org/10.1016/j.bbapap.2020.140536

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• Understanding the reaction mechanism of chlorite dismutases: Characterizing protonation states of turnover-associated amino acid residues using neutron cryo-crystallography

  Source: Schmidt D, Schaffner I, Mlynek G, Djinovic-Carugo K, Obinger C. Understanding the reaction mechanism of chlorite dismutases: Characterizing protonation states of turnover-associated amino acid residues using neutron cryo-crystallography. In: Müller M, Müller-Buschbaum P , editors. MLZ Neutrons 2021. 2021.

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• Arresting the Catalytic Arginine in Chlorite Dismutases: Impact on Heme Coordination, Thermal Stability, and Catalysis.

  Source: Schmidt D, Serra I, Mlynek G, Pfanzagl V, Hofbauer S, Furtmüller P, et al. Arresting the Catalytic Arginine in Chlorite Dismutases: Impact on Heme Coordination, Thermal Stability, and Catalysis. Biochemistry. 2021;60(8):621-34. doi:https://doi.org/10.1021/acs.biochem.0c00910

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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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• 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 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.

  Conference & Workshop proceedings, paper, abstract

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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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• Molecular Mechanism of Enzymatic Chlorite Degradation

  Source: Obinger C, Schaffner I, Schmidt D, Smulevich G, Coates L, Battistuzzi G, et al. Molecular Mechanism of Enzymatic Chlorite Degradation. In: Freisinger E, Sigel R , editors. ICBIC 19. 2019.

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• Manipulation of heme environment in the active site of chlorite dismutases and its impact on the enzymatic activity

  Source: Schmidt D, Schaffner I, Hofbauer S, Furtmüller PG, Obinger C. Manipulation of heme environment in the active site of chlorite dismutases and its impact on the enzymatic activity. In: Freisinger E, Sigel R , editors. ICBIC 19. 2019.

  Conference & Workshop proceedings, paper, abstract

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• Characterization and comparison of the distal heme environment of dimeric and pentameric chlorite dismutases

  Source: Schmidt, D, Schaffner, I, Hofbauer, S, et al. Characterization and comparison of the distal heme environment of dimeric and pentameric chlorite dismutases. In: C Queen’s University Belfast A , editor. OxyZymes 2018 [Internet]. 2018. Available from: https://www.qub.ac.at/sites/oxyzymes-conf-2018

  Conference & Workshop proceedings, paper, abstract

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  www.qub.ac.at