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The Role of the Hydrogen Bond Network in Maintaining Heme Pocket Stability and Protein Function Specificity of C. diphtheriae Coproheme Decarboxylase

Autor: Federico Sebastiani, Chiara Baroni, Gaurav Patil, Andrea Dali, Maurizio Becucci, Stefan Hofbauer, Giulietta Smulevich

Publikováno v: Biomolecules, Vol 13, Iss 2, p 235 (2023)

Monoderm bacteria accumulate heme b via the coproporphyrin-dependent biosynthesis pathway. In the final step, in the presence of two molecules of H2O2, the propionate groups of coproheme at positions 2 and 4 are decarboxylated to form vinyl groups by

Externí odkaz: https://doaj.org/article/e289eb301f1b4da7b7af116ec4537c9b

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The combination of resonance Raman spectroscopy and site directed mutagenesis to study the diverse aspects of heme protein structure and function

Autor: Federico Sebastiani, Andrea Dali, Giulietta Smulevich

Publikováno v: Journal of Porphyrins and Phthalocyanines. 26:755-764

This review provides examples illustrating the powerful combination of resonance Raman spectroscopy and site-directed mutagenesis to investigate the structure-function relationship in structurally different heme proteins with diverse physiological fu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::bfe6fb6ca4982b39ebb0e7b81ddb1984
https://doi.org/10.1142/s1088424622300026

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

Autor: Andrea Dali, Thomas Gabler, Federico Sebastiani, Alina Destinger, Paul Georg Furtmüller, Vera Pfanzagl, Maurizio Becucci, Giulietta Smulevich, Stefan Hofbauer

Publikováno v: Protein Science. 32

Coproporphyrin ferrochelatases (CpfCs) are enzymes catalyzing the penultimate step in the coproporphyrin-dependent (CPD) heme biosynthesis pathway, which is mainly utilized by monoderm bacteria. Ferrochelatases insert ferrous iron into a porphyrin ma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4075326a5761cc5a564bd7942257f79
https://doi.org/10.1002/pro.4534

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

Autor: Johannes Helm, Thomas Gabler, Andrea Dali, Giulietta Smulevich, Federico Sebastiani, Paul G. Furtmüller, Christian Obinger, Stefan Hofbauer

Publikováno v: The FEBS Journal. 289:1680-1699

Coproporpyhrin III is the substrate of coproporphyrin ferrochelatases (CpfCs). These enzymes catalyse the insertion of ferrous iron into the porphyrin ring. This is the penultimate step within the coproporphyrin-dependent haeme biosynthesis pathway.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e190fea7aacb1109a2a7516867ff5f6
https://doi.org/10.1111/febs.16257

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The role of the distal cavity in carbon monoxide stabilization in the coproheme decarboxylase enzyme from C. diphtheriae

Autor: Federico Sebastiani, Andrea Dali, Diego Javier Alonso de Armiño, Lorenzo Campagni, Gaurav Patil, Maurizio Becucci, Stefan Hofbauer, Dario A. Estrin, Giulietta Smulevich

Publikováno v: Journal of Inorganic Biochemistry. 245:112243

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::502a1130eaf68efa03cd075c46c7b0f1
https://doi.org/10.1016/j.jinorgbio.2023.112243

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Author response for 'Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen‐bonding interactions of the four propionate groups'

Autor: Stefan Hofbauer, Federico Sebastiani, Thomas Gabler, Giulietta Smulevich, Christian Obinger, Andrea Dali, Paul G. Furtmüller, Johannes Helm

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fa87162b92ef8ce63d77d0a344ce5af4
https://doi.org/10.1111/febs.16257/v2/response1

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