Relevant bibliographies by topics / Coproheme Decarboxylase

Academic literature on the topic 'Coproheme Decarboxylase'

Author: Grafiati
Published: 10 March 2023

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Journal articles on the topic "Coproheme Decarboxylase"

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Zhang, Ying, Junkai Wang, Chang Yuan, Wei Liu, Hongwei Tan, Xichen Li, and Guangju Chen. "Ruffling drives coproheme decarboxylation by facilitating PCET: a theoretical investigation of ChdC." Physical Chemistry Chemical Physics 22, no. 28 (2020): 16117–24. http://dx.doi.org/10.1039/d0cp02690e.

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Coproheme decarboxylase (ChdC) is an essential enzyme in the coproporphyrin-dependent heme synthesis pathway, which catalyzes oxidative decarboxylation of coproheme at the positions p2 and p4 to generate heme b under the action of hydrogen peroxide.
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Liu, Wei, Yunjie Pang, Yutian Song, Xichen Li, Hongwei Tan, and Guangju Chen. "Reorienting Mechanism of Harderoheme in Coproheme Decarboxylase—A Computational Study." International Journal of Molecular Sciences 23, no. 5 (February 25, 2022): 2564. http://dx.doi.org/10.3390/ijms23052564.

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Coproheme decarboxylase (ChdC) is an important enzyme in the coproporphyrin-dependent pathway (CPD) of Gram-positive bacteria that decarboxylates coproheme on two propionates at position 2 and position 4 sequentially to generate heme b by using H2O2 as an oxidant. This work focused on the ChdC from Geobacillus stearothermophilus (GsChdC) to elucidate the mechanism of its sequential two-step decarboxylation of coproheme. The models of GsChdC in a complex with substrate and reaction intermediate were built to investigate the reorienting mechanism of harderoheme. Targeted molecular dynamics simulations on these models validated that harderoheme is able to rotate in the active site of GsChdC with a 19.06-kcal·mol−1 energy barrier after the first step of decarboxylation to bring the propionate at position 4 in proximity of Tyr145 to continue the second decarboxylation step. The harderoheme rotation mechanism is confirmed to be much easier than the release–rebinding mechanism. In the active site of GsChdC, Trp157 and Trp198 comprise a “gate” construction to regulate the clockwise rotation of the harderoheme. Lys149 plays a critical role in the rotation mechanism, which not only keeps the Trp157–Trp198 “gate” from being closed but also guides the propionate at position 4 through the gap between Trp157 and Trp198 through a salt bridge interaction.
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3

Sebastiani, Federico, Chiara Baroni, Gaurav Patil, Andrea Dali, Maurizio Becucci, Stefan Hofbauer, and Giulietta Smulevich. "The Role of the Hydrogen Bond Network in Maintaining Heme Pocket Stability and Protein Function Specificity of C. diphtheriae Coproheme Decarboxylase." Biomolecules 13, no. 2 (January 25, 2023): 235. http://dx.doi.org/10.3390/biom13020235.

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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 coproheme decarboxylase (ChdC), in a stepwise process. Decarboxylation of propionate 2 produces an intermediate that rotates by 90° inside the protein pocket, bringing propionate 4 near the catalytic tyrosine, to allow the second decarboxylation step. The active site of ChdCs is stabilized by an extensive H-bond network involving water molecules, specific amino acid residues, and the propionate groups of the porphyrin. To evaluate the role of these H-bonds in the pocket stability and enzyme functionality, we characterized, via resonance Raman and electronic absorption spectroscopies, single and double mutants of the actinobacterial pathogen Corynebacterium diphtheriae ChdC complexed with coproheme and heme b. The selective elimination of the H-bond interactions between propionates 2, 4, 6, and 7 and the polar residues of the pocket allowed us to establish the role of each H-bond in the catalytic reaction and to follow the changes in the interactions from the substrate to the product.
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Milazzo, Lisa, Thomas Gabler, Vera Pfanzagl, Hanna Michlits, Paul G. Furtmüller, Christian Obinger, Stefan Hofbauer, and Giulietta Smulevich. "The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis." Journal of Inorganic Biochemistry 195 (June 2019): 61–70. http://dx.doi.org/10.1016/j.jinorgbio.2019.03.009.

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Milazzo, Lisa, Stefan Hofbauer, Barry D. Howes, Thomas Gabler, Paul G. Furtmüller, Christian Obinger, and Giulietta Smulevich. "Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes." Biochemistry 57, no. 13 (March 14, 2018): 2044–57. http://dx.doi.org/10.1021/acs.biochem.8b00186.

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6

Streit, Bennett R., Arianna I. Celis, Krista Shisler, Kenton R. Rodgers, Gudrun S. Lukat-Rodgers, and Jennifer L. DuBois. "Reactions of Ferrous Coproheme Decarboxylase (HemQ) with O2 and H2O2 Yield Ferric Heme b." Biochemistry 56, no. 1 (December 16, 2016): 189–201. http://dx.doi.org/10.1021/acs.biochem.6b00958.

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7

Sebastiani, Federico, Riccardo Risorti, Chiara Niccoli, Hanna Michlits, Maurizio Becucci, Stefan Hofbauer, and Giulietta Smulevich. "An active site at work – the role of key residues in C. diphteriae coproheme decarboxylase." Journal of Inorganic Biochemistry 229 (April 2022): 111718. http://dx.doi.org/10.1016/j.jinorgbio.2022.111718.

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8

Celis, Arianna I., George H. Gauss, Bennett R. Streit, Krista Shisler, Garrett C. Moraski, Kenton R. Rodgers, Gudrun S. Lukat-Rodgers, John W. Peters, and Jennifer L. DuBois. "Structure-Based Mechanism for Oxidative Decarboxylation Reactions Mediated by Amino Acids and Heme Propionates in Coproheme Decarboxylase (HemQ)." Journal of the American Chemical Society 139, no. 5 (January 27, 2017): 1900–1911. http://dx.doi.org/10.1021/jacs.6b11324.

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9

Tian, Ge, Gangping Hao, Xiaohua Chen, and Yongjun Liu. "Tyrosyl Radical-Mediated Sequential Oxidative Decarboxylation of Coproporphyrinogen III through PCET: Theoretical Insights into the Mechanism of Coproheme Decarboxylase ChdC." Inorganic Chemistry 60, no. 17 (August 12, 2021): 13539–49. http://dx.doi.org/10.1021/acs.inorgchem.1c01864.

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10

Pfanzagl, Vera, Laurenz Holcik, Daniel Maresch, Giulia Gorgone, Hanna Michlits, Paul G. Furtmüller, and Stefan Hofbauer. "Coproheme decarboxylases - Phylogenetic prediction versus biochemical experiments." Archives of Biochemistry and Biophysics 640 (February 2018): 27–36. http://dx.doi.org/10.1016/j.abb.2018.01.005.

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Dissertations / Theses on the topic "Coproheme Decarboxylase"

1

Milazzo, Lisa. "How resonance Raman spectroscopy can give valuable insights into diverse aspects of heme protein structure and function." Doctoral thesis, 2019. http://hdl.handle.net/2158/1154362.

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Resonance Raman (RR) spectroscopy complemented by UV-Vis absorption spectroscopy is a very powerful technique to investigate the structure-function relationships of heme proteins, a widely distributed and biological relevant class of proteins which can play different biological functions. Since the protein activity is tightly linked to the structure of the heme active site, my study has been devoted to the investigation of several heme proteins involved in important biological processes, to obtain a comprehensive spectroscopic signature, with the aim to highlight the relationship between the heme pocket architecture and the protein function. The studies were carried out on native proteins and selected site-directed mutants, at both room (298 K) and low (80 K) temperature, at various pH, and in presence of various exogenous ligands, spanning the excitation wavelengths from UV to the visible region.
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