Cargando…

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

[Image: see text] Chlorite dismutases (Clds) are heme b-containing oxidoreductases that can decompose chlorite to chloride and molecular oxygen. They are divided in two clades that differ in oligomerization, subunit architecture, and the hydrogen-bonding network of the distal catalytic arginine, whi...

Descripción completa

Detalles Bibliográficos
Autores principales:	Schmidt, Daniel, Serra, Ilenia, Mlynek, Georg, Pfanzagl, Vera, Hofbauer, Stefan, Furtmüller, Paul G., Djinović-Carugo, Kristina, Van Doorslaer, Sabine, Obinger, Christian
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	American Chemical Society 2021
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7931450/ https://www.ncbi.nlm.nih.gov/pubmed/33586945 http://dx.doi.org/10.1021/acs.biochem.0c00910

Ejemplares similares

Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine
por: Schmidt, Daniel, et al.
Publicado: (2023)

Structure and heme-binding properties of HemQ (chlorite dismutase-like protein) from Listeria monocytogenes
por: Hofbauer, Stefan, et al.
Publicado: (2015)

Impact of subunit and oligomeric structure on the thermal and conformational stability of chlorite dismutases
por: Hofbauer, Stefan, et al.
Publicado: (2012)

Manipulating Conserved Heme Cavity Residues of Chlorite Dismutase: Effect on Structure, Redox Chemistry, and Reactivity
por: Hofbauer, Stefan, et al.
Publicado: (2013)

Chlorite dismutases – a heme enzyme family for use in bioremediation and generation of molecular oxygen
por: Hofbauer, Stefan, et al.
Publicado: (2014)

From chlorite dismutase towards HemQ–the role of the proximal H-bonding network in haeme binding
por: Hofbauer, Stefan, et al.
Publicado: (2016)

Dimeric chlorite dismutase from the nitrogen‐fixing cyanobacterium C yanothece sp. PCC7425
por: Schaffner, Irene, et al.
Publicado: (2015)

Redox Thermodynamics of High-Spin and Low-Spin Forms of Chlorite Dismutases with Diverse Subunit and Oligomeric Structures
por: Hofbauer, Stefan, et al.
Publicado: (2012)

Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage
por: Pfanzagl, Vera, et al.
Publicado: (2018)

Mechanism of reaction of chlorite with mammalian heme peroxidases
por: Jakopitsch, Christa, et al.
Publicado: (2014)

Transiently Produced Hypochlorite Is Responsible for the Irreversible Inhibition of Chlorite Dismutase
por: Hofbauer, Stefan, et al.
Publicado: (2014)

Molecular Mechanism of Enzymatic Chlorite Detoxification: Insights from Structural and Kinetic Studies
por: Schaffner, Irene, et al.
Publicado: (2017)

Secreted heme peroxidase from Dictyostelium discoideum: Insights into catalysis, structure, and biological role
por: Nicolussi, Andrea, et al.
Publicado: (2018)

Investigation of Ion Binding in Chlorite Dismutases by Means of Molecular Dynamics Simulations
por: Sündermann, Axel, et al.
Publicado: (2014)

Crystal structures and calorimetry reveal catalytically relevant binding mode of coproporphyrin and coproheme in coproporphyrin ferrochelatase
por: Hofbauer, Stefan, et al.
Publicado: (2019)

Hydrogen peroxide‐mediated conversion of coproheme to heme b by HemQ—lessons from the first crystal structure and kinetic studies
por: Hofbauer, Stefan, et al.
Publicado: (2016)

Chemistry and Molecular Dynamics Simulations of Heme b-HemQ and Coproheme-HemQ
por: Hofbauer, Stefan, et al.
Publicado: (2016)

Redox Cofactor Rotates during Its Stepwise Decarboxylation: Molecular Mechanism of Conversion of Coproheme to Heme b
por: Milazzo, Lisa, et al.
Publicado: (2019)

Unexpected photosensitivity of the well-characterized heme enzyme chlorite dismutase
por: Mahor, Durga, et al.
Publicado: (2020)

Unique Biradical Intermediate in the Mechanism of the Heme Enzyme Chlorite Dismutase
por: Püschmann, Julia, et al.
Publicado: (2021)

Actinobacterial Coproheme Decarboxylases Use Histidine as a Distal Base to Promote Compound I Formation
por: Michlits, Hanna, et al.
Publicado: (2020)

In Vitro Heme Coordination of a Dye-Decolorizing Peroxidase—The Interplay of Key Amino Acids, pH, Buffer and Glycerol
por: Nys, Kevin, et al.
Publicado: (2021)

The hydrogen bonding network of coproheme in coproheme decarboxylase from Listeria monocytogenes: Effect on structure and catalysis
por: Milazzo, Lisa, et al.
Publicado: (2019)

On the Track of Long-Range Electron Transfer in B-Type Dye-Decolorizing Peroxidases: Identification of a Tyrosyl Radical by Computational Prediction and Electron Paramagnetic Resonance Spectroscopy
por: Nys, Kevin, et al.
Publicado: (2021)

Characterizing Isozymes of Chlorite Dismutase for Water Treatment
por: Mobilia, Kellen C., et al.
Publicado: (2017)

Posttranslational modification and heme cavity architecture of human eosinophil peroxidase—insights from first crystal structure and biochemical characterization
por: Pfanzagl, Vera, et al.
Publicado: (2023)

Understanding molecular enzymology of porphyrin-binding α + β barrel proteins - One fold, multiple functions
por: Hofbauer, Stefan, et al.
Publicado: (2021)

The staphylococcal inhibitory protein SPIN binds to human myeloperoxidase with picomolar affinity but only dampens halide oxidation
por: Leitgeb, Urban, et al.
Publicado: (2022)

Independent evolution of four heme peroxidase superfamilies
por: Zámocký, Marcel, et al.
Publicado: (2015)

A Dimeric Chlorite Dismutase Exhibits O(2)-Generating Activity and Acts as a Chlorite Antioxidant in Klebsiella pneumoniae MGH 78578
por: Celis, Arianna I., et al.
Publicado: (2014)

A traffic light enzyme: acetate binding reversibly switches chlorite dismutase from a red- to a green-colored heme protein
por: Mahor, Durga, et al.
Publicado: (2020)

Reaction intermediate rotation during the decarboxylation of coproheme to heme b in C. diphtheriae
por: Sebastiani, Federico, et al.
Publicado: (2021)

Turning points in the evolution of peroxidase–catalase superfamily: molecular phylogeny of hybrid heme peroxidases
por: Zámocký, Marcel, et al.
Publicado: (2014)

Two-faced Fcab prevents polymerization with VEGF and reveals thermodynamics and the 2.15 Å crystal structure of the complex
por: Lobner, Elisabeth, et al.
Publicado: (2017)

Structure of human promyeloperoxidase (proMPO) and the role of the propeptide in processing and maturation
por: Grishkovskaya, Irina, et al.
Publicado: (2017)

Agaricus meleagris pyranose dehydrogenase: Influence of covalent FAD linkage on catalysis and stability
por: Krondorfer, Iris, et al.
Publicado: (2014)

Heterologous expression of the gene for chlorite dismutase from Ideonella dechloratans is induced by an FNR‐type transcription factor
por: Rova, Maria, et al.
Publicado: (2020)

Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis
por: Falb, Nikolaus, et al.
Publicado: (2023)

Common Reactivity and Properties of Heme Peroxidases: A DFT Study of Their Origin
por: Ramos, Daniel R., et al.
Publicado: (2023)

Toxicological effects of chlorite in the mouse.
por: Moore, G S, et al.
Publicado: (1982)

Cannot write session to /tmp/vufind_sessions/sess_ao6iqhjbsdr3m633adjmd5uk7n