Search results for "Cytochrome"

showing 10 items of 607 documents

Inhibitory effects and oxidation of 6-methylcoumarin, 7-methylcoumarin and 7-formylcoumarin via human CYP2A6 and its mouse and pig orthologous enzymes

2015

1. Information about the metabolism of compounds is essential in drug discovery and development, risk assessment of chemicals and further development of predictive methods. 2. In vitro and in silico methods were applied to evaluate the metabolic and inhibitory properties of 6-methylcoumarin, 7-methylcoumarin and 7-formylcoumarin with human CYP2A6, mouse CYP2A5 and pig CYP2A19. 3. 6-Methylcoumarin was oxidized to fluorescent 7-hydroxy-6-methylcoumarin by CYP2A6 (Km: 0.64-0.91 µM; Vmax: 0.81-0.89 min(-1)) and by CYP2A5 and CYP2A19. The reaction was almost completely inhibited at 10 µM 7-methylcoumarin in liver microsomes of human and mouse, but in pig only 40% inhibition was obtained with the…

Models Molecular0301 basic medicineenzyme assayTime Factorscoumarin derivativecytochrome P450Health Toxicology and MutagenesisIn silicoSus scrofaHydroxylationToxicologyta3111BiochemistryCytochrome P-450 CYP2A6Inhibitory Concentration 50Mice03 medical and health sciencesCoumarinsmedicineAnimalsCytochrome P-450 Enzyme InhibitorsHumansCYP2A6ta317Pharmacologychemistry.chemical_classificationbiologyMethoxsalenta1182Cytochrome P450General MedicineMetabolismMolecular biologyIn vitroEnzyme assayKinetics030104 developmental biologyEnzymeBiochemistrychemistrybiology.proteinfluorescenceOxidation-Reductionmetabolismmedicine.drugXenobiotica
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Fe- but not Mg-protophorphyrin IX binds to a transmembrane b-type cytochrome.

2013

Transmembrane b-type cytochromes, which are crucially involved in electron transfer chains, bind one or more heme (Fe-protoporphyrin IX) molecules non-covalently. Similarly, chlorophylls are typically also non-covalently bound by several membrane integral polypeptides involved in photosynthesis. While both, chlorophyll and heme, are tetrapyrrole macrocycles, they have different substituents at the tetrapyrrole ring moiety. Furthermore, the central metal ion is Mg(2+) in chlorophyll and Fe(2+/3+) in heme. As heme and chlorophyll a have similar structures and might both be ligated by two histidine residues of a polypeptide chain, and as the local concentration of chlorophyll a might be up to …

Models MolecularChlorophyll aCytochromebiologyChemistryStereochemistryIronProtoporphyrinsCell BiologyHemeCytochromes bPhotochemistryTetrapyrroleElectron transferchemistry.chemical_compoundChlorophyllbiology.proteinMoietyMagnesiumMolecular BiologyHemeHistidineMolecular membrane biology
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SDS-facilitated in vitro formation of a transmembrane B-type cytochrome is mediated by changes in local pH.

2011

Abstract The folding and stabilization of α-helical transmembrane proteins are still not well understood. Following cofactor binding to a membrane protein provides a convenient method to monitor the formation of appropriate native structures. We have analyzed the assembly and stability of the transmembrane cytochrome b 559 ′, which can be efficiently assembled in vitro from a heme-binding PsbF homo-dimer by combining free heme with the apo-cytochrome b 559 ′. Unfolding of the protein dissolved in the mild detergent dodecyl maltoside may be induced by addition of SDS, which at high concentrations leads to dimer dissociation. Surprisingly, absorption spectroscopy reveals that heme binding and…

Models MolecularCofactor bindingProtein FoldingHeme bindingCytochromebiologyChemistryCytochrome bSpectrum AnalysisMembrane ProteinsSodium Dodecyl SulfateHemeCytochromes bHydrogen-Ion ConcentrationTransmembrane proteinchemistry.chemical_compoundBiochemistryStructural Biologybiology.proteinHumansProtein foldingMolecular BiologyHemeHistidineProtein BindingJournal of molecular biology
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Heme Binding Constricts the Conformational Dynamics of the Cytochrome b559′ Heme Binding Cavity

2012

Cytochrome b(559)' is a transmembrane protein formed by homodimerization of the 44-residue PsbF polypeptide and noncovalent binding of a heme cofactor. The PsbF polypeptide can dimerize in the absence and presence of heme. To monitor structural alterations associated with binding of heme to the apo-cytochrome, we analyzed the apo- and holo-cytochrome structure by electron paramagnetic resonance spectroscopy. Spin labeling of amino acids located close to the heme binding domain of the cytochrome revealed that the structure of the heme binding domain is unconstrained in the absence of heme. Heme binding restricts the conformational dynamics of the heme binding domain, resulting in the structu…

Models MolecularHemeproteinCytochromeHeme bindingMolecular Sequence DataHemePlasma protein bindingBiochemistryProtein Structure SecondaryCofactorchemistry.chemical_compoundApoenzymesAmino Acid SequenceGlycophorinsHemebiologyCytochrome bCell MembraneElectron Spin Resonance SpectroscopyTemperaturePhotosystem II Protein ComplexSite-directed spin labelingCytochrome b GroupProtein Structure Tertiarychemistrybiology.proteinBiophysicsSpin LabelsPeptidesProtein BindingBiochemistry
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A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer

2012

AbstractWhen localized adjacent to a Pro-kink, Thr and Ser residues can form hydrogen bonds between their polar hydroxyl group and a backbone carbonyl oxygen and thereby modulate the actual bending angle of a distorted transmembrane α-helix. We have used the homo-dimeric transmembrane cytochrome b559′ to analyze the potential role of a highly conserved Ser residue for assembly and stabilization of transmembrane proteins. Mutation of the conserved Ser residue to Ala resulted in altered heme binding properties and in increased stability of the holo-protein, most likely by tolerating subtle structural rearrangements upon heme binding. The results suggest a crucial impact of an intrahelical Ser…

Models MolecularProlineHeme bindingStereochemistryDimerMolecular ConformationBiophysicsCofactor bindingHemeBiochemistryProtein Structure Secondarychemistry.chemical_compoundProtein structureProtein stabilitySerineProtein foldingCofactor bindingHydrogen bondCell MembranePhotosystem II Protein ComplexHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinProtein Structure TertiaryOxygenTransmembrane domainHelix interactionchemistrySpectrophotometryMembrane proteinMutationTransmembrane helixProtein foldingDimerizationProtein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Cytochrome c in a Dry Trehalose Matrix: Structural and Dynamical Effects Probed by X-Ray Absorption Spectroscopy

2007

AbstractWe report on the structure and dynamics of the Fe ligand cluster of reduced horse heart cytochrome c in solution, in a dried polyvinyl alcohol (PVA) film, and in two trehalose matrices characterized by different contents of residual water. The effect of the solvent/matrix environment was studied at room temperature using Fe K-edge x-ray absorption fine structure (XAFS) spectroscopy. XAFS data were analyzed by combining ab initio simulations and multi-parameter fitting in an attempt to disentangle structural from disorder parameters. Essentially the same structural and disorder parameters account adequately for the XAFS spectra measured in solution, both in the absence and in the pre…

Models MolecularProtein ConformationIronAb initioBiophysicsHemechemistry.chemical_compoundProtein structureImidazoleAnimalsHistidineHorsesSpectroscopyX-ray absorption spectroscopyMyocardiumSpectrum AnalysisX-RaysProteinsCytochromes cTrehaloseTrehaloseX-ray absorption fine structureSolutionsCrystallographychemistryPolyvinyl AlcoholAbsorption (chemistry)Biophysical Journal
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Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding

2013

AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembrane α-helices. However, as the sequence context is crucial to determine specificity in transmembrane helix–helix interaction, the question arises how small a sequence can be without losing specificity. In the present analysis, six amino acids have been identified in the PsbF transmembrane helix dimer, which form the contact region of two interacting helices and are directly involved in helix–helix interactions. However, individual amino acids within the complex sequence pattern only together ensure sequence specificity of the analyzed transmembrane helix–helix interactions by mediating close pa…

Models MolecularStereochemistryDimerRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsCytochrome b559Sequence (biology)Context (language use)Cytochrome b559BiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundBacterial ProteinsStructural BiologyGeneticsEscherichia coliProtein Interaction Domains and MotifsAmino Acid SequenceDimerization motifMolecular Biologychemistry.chemical_classificationSequence contextHydrogen bondProtein StabilityCell MembraneMembrane ProteinsHelix–helix interactionHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinTransmembraneAmino acidTransmembrane domainchemistryDimerizationProtein BindingFEBS Letters
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Development of new Coumarin-based profluorescent substrates for human cytochrome P450 enzymes

2018

Cytochrome P450 (CYP) enzymes constitute an essential xenobiotic metabolizing system that regulates the elimination of lipophilic compounds from the body. Convenient and affordable assays for CYP enzymes are important for assessing these metabolic pathways.In this study, 10 novel profluorescent coumarin derivatives with various substitutions at carbons 3, 6 and 7 were developed. Molecular modeling indicated that 3-phenylcoumarin offers an excellent scaffold for the development of selective substrate compounds for various human CYP forms, as they could be metabolized to fluorescent 7-hydroxycoumarin derivatives. Oxidation of profluorescent coumarin derivatives to fluorescent metabolites by 1…

Models MolecularentsyymitoxidationHealth Toxicology and MutagenesisToxicology030226 pharmacology & pharmacyBiochemistrycoumarinFluorescence03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCytochrome P-450 Enzyme SystemCoumarinsCYPenzyme kineticsderivativeCytochrome P-450 Enzyme InhibitorsHumansheterocyclic compoundsEnzyme kineticskumariiniCYP2A6ta317Pharmacologychemistry.chemical_classificationBenzoflavonesbiologyChemistryCYP1A2fluoresenssiCytochrome P450substraatit (kemia)General MedicineCoumarindrug metabolismMolecular Docking SimulationMetabolic pathwayKineticsEnzymeBiochemistrylääkekemia030220 oncology & carcinogenesisInactivation Metabolicbiology.proteinMicrosomes LiverOxidation-ReductionDrug metabolism
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Rational design of allosteric modulators of the aromatase enzyme: An unprecedented therapeutic strategy to fight breast cancer.

2019

Estrogens play a key role in cellular proliferation of estrogen-receptor-positive (ER+) breast cancers (BCs). Suppression of estrogen production by competitive inhibitors of the enzyme aromatase (AIs) is currently one of the most effective therapies against ER + BC. Yet, the development of acquired resistance, after prolonged treatments with AIs, represents a clinical major concern. Serendipitous findings indicate that aromatase may be non-competitively inhibited by clinically employed drugs and/or industrial chemicals. Here, by performing in silico screening on two putative allosteric sites, molecular dynamics and free energy simulations, supported by enzymatic and cell-based assays, we id…

Molecular dynamicmedicine.drug_classIn silicoAllosteric regulationCytochromes P450; Aromatase; Molecular dynamics; Aromatase inhibitors; Docking; Breast cancer; Resistance onset; Mixed inhibition mechanismAntineoplastic AgentsBreast NeoplasmsMolecular dynamicsMolecular Dynamics SimulationDockingStructure-Activity RelationshipBreast cancerBreast cancerAromataseAllosteric RegulationCell Line TumorDrug DiscoverymedicineResistance onsetHumansMixed inhibition mechanismAromataseEnzyme InhibitorsCell ProliferationPharmacologychemistry.chemical_classificationbiologyDose-Response Relationship DrugMolecular StructureChemistryOrganic ChemistryRational designAromatase inhibitorGeneral Medicinemedicine.diseaseEnzymeAromatase inhibitorsSettore CHIM/03 - Chimica Generale E InorganicaEstrogenDocking (molecular)Drug Designbiology.proteinCancer researchDrug Screening Assays AntitumorCytochromes P450European journal of medicinal chemistry
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Suitability ofMMGBSAfor the selection of correct ligand binding modes from docking results

2018

The estimation of the correct binding mode and affinity of a ligand into a target protein using computational methods is challenging. However, docking can introduce poses from which the correct binding mode could be identified using other methods. Here, we analyzed the reliability of binding energy estimation using the molecular mechanics-generalized Born surface area (MMGBSA) method without and with energy minimization to identify the likely ligand binding modes within docking results. MMGBSA workflow (a) outperformed docking in recognizing the correct binding modes of androgen receptor ligands and (b) improved the correlation coefficient of computational and experimental results of rescor…

Molecular modelBinding energyta3111LigandsEnergy minimization01 natural sciencesBiochemistrylääkesuunnitteluSubstrate SpecificityCytochrome P-450 CYP2A6Free energy perturbationCoumarinsDrug DiscoveryHumansta317PharmacologyBinding Sitesmolecular modeling010405 organic chemistryChemistryDrug discoveryOrganic Chemistryta1182liganditreceptor and ligandslaskennallinen kemiaLigand (biochemistry)Protein Structure Tertiary0104 chemical sciencesMolecular Docking Simulation010404 medicinal & biomolecular chemistryDocking (molecular)structure based drug-designThermodynamicsMolecular MedicineproteiinitTarget proteinBiological systemProtein BindingChemical Biology & Drug Design
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