Paul G. Furtmüller
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View article: Halide binding by myeloperoxidase is regulated by access channel dynamics and charge interactions
Halide binding by myeloperoxidase is regulated by access channel dynamics and charge interactions Open
The heme enzyme myeloperoxidase is a key player in the innate immune defense. It uses hydrogen peroxide to produce bactericidal hypohalous acids from (pseudo)halides, foremost chloride, and thiocyanate in the neutrophil phagosome. However,…
View article: Coproheme decarboxylase from Bacillus subtilis is required for bacterial growth and heme b biosynthesis under anaerobic conditions
Coproheme decarboxylase from Bacillus subtilis is required for bacterial growth and heme b biosynthesis under anaerobic conditions Open
Heme biosynthesis notably does not follow a universal pathway. Instead, different organisms utilize various routes of producing this essential molecule. The coproporphyrin-dependent (CPD) pathway is unique to Gram-positive bacteria. Given …
View article: One single hydrogen bond guarantees conformational stability and activity in coproheme decarboxylase from Corynebacterium diphtheriae
One single hydrogen bond guarantees conformational stability and activity in coproheme decarboxylase from Corynebacterium diphtheriae Open
Active site architectures of enzymes are defined by many interactions between substrate and amino acid residues and are optimized for specific and efficient substrate turnover. In the case of coproheme decarboxylase (ChdC) the active site …
View article: Insights into the flexibility of the domain‐linking loop in actinobacterial coproheme decarboxylase through structures and molecular dynamics simulations
Insights into the flexibility of the domain‐linking loop in actinobacterial coproheme decarboxylase through structures and molecular dynamics simulations Open
Prokaryotic heme biosynthesis in Gram‐positive bacteria follows the coproporphyrin‐dependent heme biosynthesis pathway. The last step in this pathway is catalyzed by the enzyme coproheme decarboxylase, which oxidatively transforms two prop…
View article: Insights into heme degradation and hydrogen peroxide-induced dimerization of human neuroglobin
Insights into heme degradation and hydrogen peroxide-induced dimerization of human neuroglobin Open
In this present study, we investigated the H2O2-induced oligomerization of wild-type human neuroglobin (hNgb) and of some selected variants (C46AC55A, Y44A, Y44F, Y44AC46AC55A, Y44AC46AC55A) to clarify how the process is affected by the Cy…
View article: Entrance channels to coproheme in coproporphyrin ferrochelatase probed by exogenous imidazole binding
Entrance channels to coproheme in coproporphyrin ferrochelatase probed by exogenous imidazole binding Open
View article: Lactoperoxidase catalytically oxidize hydrogen sulfide via intermediate formation of sulfheme derivatives
Lactoperoxidase catalytically oxidize hydrogen sulfide via intermediate formation of sulfheme derivatives Open
View article: Revisiting catalytic His and Glu residues in coproporphyrin ferrochelatase – unexpected activities of active site variants
Revisiting catalytic His and Glu residues in coproporphyrin ferrochelatase – unexpected activities of active site variants Open
The identification of the coproporphyrin‐dependent heme biosynthetic pathway, which is used almost exclusively by monoderm bacteria in 2015 by Dailey et al . triggered studies aimed at investigating the enzymes involved in this pathway tha…
View article: An Automated pre-Dilution Setup for Von Willebrand Factor Activity Assays
An Automated pre-Dilution Setup for Von Willebrand Factor Activity Assays Open
Accurate quantification of von Willebrand factor ristocetin cofactor activity (VWF:RCo) is critical for the diagnosis and classification of von Willebrand disease, the most common hereditary and acquired bleeding disorder in humans. Moreov…
View article: Peroxidasin Inhibition by Phloroglucinol and Other Peroxidase Inhibitors
Peroxidasin Inhibition by Phloroglucinol and Other Peroxidase Inhibitors Open
Human peroxidasin (PXDN) is a ubiquitous peroxidase enzyme expressed in most tissues in the body. PXDN represents an interesting therapeutic target for inhibition, as it plays a role in numerous pathologies, including cardiovascular diseas…
View article: The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes
The Molecular Evolution, Structure, and Function of Coproporphyrinogen Oxidase and Protoporphyrinogen Oxidase in Prokaryotes Open
Coproporphyrinogen oxidase (CgoX) and protoporphyrinogen oxidase (PgoX) catalyze the oxidation of the flexible cyclic tetrapyrrole of porphyrinogen compounds into fully conjugated, planar macrocyclic porphyrin compounds during heme biosynt…
View article: Antibody fragments functionalized with non-canonical amino acids preserving structure and functionality - A door opener for new biological and therapeutic applications
Antibody fragments functionalized with non-canonical amino acids preserving structure and functionality - A door opener for new biological and therapeutic applications Open
Functionalization of proteins by incorporating reactive non-canonical amino acids (ncAAs) has been widely applied for numerous biological and therapeutic applications. The requirement not to lose the intrinsic properties of these proteins …
View article: Posttranslational modification and heme cavity architecture of human eosinophil peroxidase—insights from first crystal structure and biochemical characterization
Posttranslational modification and heme cavity architecture of human eosinophil peroxidase—insights from first crystal structure and biochemical characterization Open
Eosinophil peroxidase (EPO) is the most abundant granule protein exocytosed by eosinophils, specialized human phagocytes. Released EPO catalyzes the formation of reactive oxidants from bromide, thiocyanate, and nitrite that kill tissue-inv…
View article: Iron insertion into coproporphyrin <scp>III</scp>‐ferrochelatase complex: Evidence for an intermediate distorted catalytic species
Iron insertion into coproporphyrin <span>III</span>‐ferrochelatase complex: Evidence for an intermediate distorted catalytic species Open
Understanding the reaction mechanism of enzymes at the molecular level is generally a difficult task, since many parameters affect the turnover. Often, due to high reactivity and formation of transient species or intermediates, detailed in…
View article: Hypochlorous acid inactivates myeloperoxidase inside phagocytosing neutrophils
Hypochlorous acid inactivates myeloperoxidase inside phagocytosing neutrophils Open
When neutrophils phagocytose bacteria, they release myeloperoxidase (MPO) into phagosomes to catalyse the conversion of superoxide to the potent antimicrobial oxidant hypochlorous acid (HOCl). Here we show that within neutrophils, MPO is i…
View article: Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme
Reactivity of Coproheme Decarboxylase with Monovinyl, Monopropionate Deuteroheme Open
Coproheme decarboxylases (ChdCs) are terminal enzymes of the coproporphyrin-dependent heme biosynthetic pathway. In this reaction, two propionate groups are cleaved from the redox-active iron-containing substrate, coproheme, to form vinyl …
View article: Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine
Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine Open
Data type: spectroscopic measurements (UV-visible, ECD, EPR), enzyme activity measurements, mass spectrometry, spectroelectrochemistry and data analysis. Files are in .DTA, .DSC, .xlsx, .m, .mat, .BSW, .csv, .txt, …
View article: Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine
Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine Open
Data type: spectroscopic measurements (UV-visible, ECD, EPR), enzyme activity measurements, mass spectrometry, spectroelectrochemistry and data analysis. Files are in .DTA, .DSC, .xlsx, .m, .mat, .BSW, .csv, .txt, …
View article: Common Reactivity and Properties of Heme Peroxidases: A DFT Study of Their Origin
Common Reactivity and Properties of Heme Peroxidases: A DFT Study of Their Origin Open
Electronic structure calculations using the density-functional theory (DFT) have been performed to analyse the effect of water molecules and protonation on the heme group of peroxidases in different redox (ferric, ferrous, compounds I and …
View article: Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine
Compound I Formation and Reactivity in Dimeric Chlorite Dismutase: Impact of pH and the Dynamics of the Catalytic Arginine Open
The heme enzyme chlorite dismutase (Cld) catalyzes the degradation of chlorite to chloride and dioxygen. Many questions about the molecular reaction mechanism of this iron protein have remained unanswered, including the electronic nature o…
View article: Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis
Structural aspects of enzymes involved in prokaryotic Gram-positive heme biosynthesis Open
View article: Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin <scp>III</scp>: Propionate interactions and porphyrin core deformation
Active site architecture of coproporphyrin ferrochelatase with its physiological substrate coproporphyrin <span>III</span>: Propionate interactions and porphyrin core deformation Open
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 p…
View article: On the Origin of the Common Reactivity and Properties of Heme Peroxidases: A DFT Study
On the Origin of the Common Reactivity and Properties of Heme Peroxidases: A DFT Study Open
Electronic structure calculations have been carried out to examine the effect of protonation and water molecules on the heme group of peroxidases in different redox (ferric, ferrous, compounds I and II) and spin states. Shared geometries, …
View article: The staphylococcal inhibitory protein SPIN binds to human myeloperoxidase with picomolar affinity but only dampens halide oxidation
The staphylococcal inhibitory protein SPIN binds to human myeloperoxidase with picomolar affinity but only dampens halide oxidation Open
View article: Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase
Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase Open
Data type: spectroscopic measurements (UV-visible, ECD, EPR), DSC measurements, X-ray crystallography datasets, kinetic measurements, Molecular Dynamics simulations and data analysis. Files are in spc, par, DTA, DS…
View article: Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase
Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase Open
Data type: spectroscopic measurements (UV-visible, ECD, EPR), DSC measurements, X-ray crystallography datasets, kinetic measurements, Molecular Dynamics simulations and data analysis. Files are in spc, par, DTA, DS…
View article: Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase
Impact of the dynamics of the catalytic arginine on nitrite and chlorite binding by dimeric chlorite dismutase Open
View article: Effect of ionizing radiation on human myeloperoxidase: Reaction with hydrated electrons
Effect of ionizing radiation on human myeloperoxidase: Reaction with hydrated electrons Open
View article: Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen‐bonding interactions of the four propionate groups
Substrate specificity and complex stability of coproporphyrin ferrochelatase is governed by hydrogen‐bonding interactions of the four propionate groups Open
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 biosynthesi…
View article: Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy
Pseudoperoxidase activity, conformational stability, and aggregation propensity of the His98Tyr myoglobin variant: implications for the onset of myoglobinopathy Open
The autosomal dominant striated muscle disease myoglobinopathy is due to the single point mutation His98Tyr in human myoglobin (MB), the heme protein responsible for binding, storage, and controlled release of O 2 in striated muscle. In or…