Cargando…

Hydrogen peroxide‐mediated conversion of coproheme to heme b by HemQ—lessons from the first crystal structure and kinetic studies

Heme biosynthesis in Gram‐positive bacteria follows a recently described coproporphyrin‐dependent pathway with HemQ catalyzing the decarboxylation of coproheme to heme b. Here we present the first crystal structure of a HemQ (homopentameric coproheme‐HemQ from Listeria monocytogenes) at 1.69 Å resol...

Descripción completa

Detalles Bibliográficos
Autores principales:	Hofbauer, Stefan, Mlynek, Georg, Milazzo, Lisa, Pühringer, Dominic, Maresch, Daniel, Schaffner, Irene, Furtmüller, Paul G., Smulevich, Giulietta, Djinović‐Carugo, Kristina, Obinger, Christian
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	John Wiley and Sons Inc. 2016
Materias:	Original Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5157759/ https://www.ncbi.nlm.nih.gov/pubmed/27758026 http://dx.doi.org/10.1111/febs.13930

Ejemplares similares

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)

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

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

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

Insights into the Active Site of Coproheme Decarboxylase from Listeria monocytogenes
por: Milazzo, Lisa, et al.
Publicado: (2018)

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

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

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

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

Spectroscopic evidence of the effect of hydrogen peroxide excess on the coproheme decarboxylase from actinobacterial Corynebacterium diphtheriae
por: Sebastiani, Federico, et al.
Publicado: (2022)

The Role of the Hydrogen Bond Network in Maintaining Heme Pocket Stability and Protein Function Specificity of C. diphtheriae Coproheme Decarboxylase
por: Sebastiani, Federico, et al.
Publicado: (2023)

Arresting the Catalytic Arginine in Chlorite Dismutases: Impact on Heme Coordination, Thermal Stability, and Catalysis
por: Schmidt, Daniel, et al.
Publicado: (2021)

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

Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme
por: Patil, Gaurav, et al.
Publicado: (2023)

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

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

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

Initial Steps to Engineer Coproheme Decarboxylase to Obtain Stereospecific Monovinyl, Monopropionyl Deuterohemes
por: Michlits, Hanna, et al.
Publicado: (2022)

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

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

The HemQ coprohaem decarboxylase generates reactive oxygen species: implications for the evolution of classical haem biosynthesis
por: Hobbs, Charlie, et al.
Publicado: (2016)

Independent evolution of four heme peroxidase superfamilies
por: Zámocký, Marcel, 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)

A conformation-specific ON-switch for controlling CAR T cells with an orally available drug
por: Zajc, Charlotte U., et al.
Publicado: (2020)

Inactivation of human myeloperoxidase by hydrogen peroxide()
por: Paumann-Page, Martina, et al.
Publicado: (2013)

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

Iron insertion into coproporphyrin III‐ferrochelatase complex: Evidence for an intermediate distorted catalytic species
por: Gabler, Thomas, et al.
Publicado: (2023)

Molecular evolution of hydrogen peroxide degrading enzymes
por: Zámocký, Marcel, et al.
Publicado: (2012)

Eukaryotic extracellular catalase–peroxidase from Magnaporthe grisea – Biophysical/chemical characterization of the first representative from a novel phytopathogenic KatG group
por: Zámocký, Marcel, et al.
Publicado: (2012)

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)

Function Coupling Mechanism of PhuS and HemO in Heme Degradation
por: Lee, Michael J. Y., et al.
Publicado: (2017)

A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins With Extreme Reactivities Toward Diatomic Gases and Nitrite
por: Villar, Irene, et al.
Publicado: (2020)

Corrigendum: A Plant Gene Encoding One-Heme and Two-Heme Hemoglobins With Extreme Reactivities Toward Diatomic Gases and Nitrite
por: Villar, Irene, et al.
Publicado: (2021)

Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin III: Propionate interactions and porphyrin core deformation
por: Dali, Andrea, et al.
Publicado: (2023)

Reorienting Mechanism of Harderoheme in Coproheme Decarboxylase—A Computational Study
por: Liu, Wei, et al.
Publicado: (2022)

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

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)

Cannot write session to /tmp/vufind_sessions/sess_avuqe6v5b1dfv2r0s1vcfr15jf