Search results for "Biliverdin"

showing 10 items of 17 documents

Protonation of the Biliverdin IXα Chromophore in the Red and Far-Red Photoactive States of a Bacteriophytochrome

2019

The tetrapyrrole chromophore biliverdin IXα (BV) in the bacteriophytochrome from Deinococcus radiodurans (DrBphP) is usually assumed to be fully protonated, but this assumption has not been systematically validated by experiments or extensive computations. Here, we use force field molecular dynamics simulations and quantum mechanics/molecular mechanics calculations with density functional theory and XMCQDPT2 methods to investigate the effect of the five most probable protonation forms of BV on structural stability, binding pocket interactions, and absorption spectra in the two photochromic states of DrBphP. While agreement with X-ray structural data and measured UV/vis spectra suggest that …

Absorption spectroscopyProtein ConformationPopulationProtonationMolecular Dynamics SimulationCrystallography X-Ray010402 general chemistryPhotochemistry01 natural sciencesArticlequantum chemistrychemistry.chemical_compoundMolecular dynamicsPhotochromismBacterial Proteins0103 physical scienceskvanttikemiaMaterials ChemistrymolekyylidynamiikkaPhysical and Theoretical Chemistryeducationta116excited statesphytochromeeducation.field_of_studyBinding SitesBiliverdin010304 chemical physicsChemistryBiliverdineta1182Chromophoremolecular dynamics3. Good health0104 chemical sciencesSurfaces Coatings and FilmsSpectrophotometry UltravioletDensity functional theoryDeinococcusvalokemiaproteiinitThe Journal of Physical Chemistry B
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Removal of Chromophore-proximal Polar Atoms Decreases Water Content and Increases Fluorescence in a Near Infrared Phytofluor

2015

Genetically encoded fluorescent markers have revolutionized cell and molecular biology due to their biological compatibility, controllable spatiotemporal expression, and photostability. To achieve in vivo imaging in whole animals, longer excitation wavelength probes are needed due to the superior ability of near infrared light to penetrate tissues unimpeded by absorbance from biomolecules or autofluorescence of water. Derived from near infrared-absorbing bacteriophytochromes, phytofluors are engineered to fluoresce in this region of the electromagnetic spectrum, although high quantum yield remains an elusive goal. An invariant aspartate residue is of utmost importance for photoconversion in…

chromophore binding domain (CBD)Analytical chemistryQuantum yieldPhotochemistryBiochemistry Genetics and Molecular Biology (miscellaneous)BiochemistryFluorescence spectroscopychemistry.chemical_compoundDeinococcus radioduransWiPhy2Side chainMolecular Biologylcsh:QH301-705.5Wisconsin infrared phytofluor (WiPhy2)Original ResearchBiliverdinta114Physicsta1182Excitation-emission matrix (EEM)ChromophorePhotobleachingFluorescenceexcitation-emission matrix (EEM)chemistrylcsh:Biology (General)Excited statetetrapyrroleFrontiers in Molecular Biosciences
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Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome

2022

Funding Information: This work was supported by Academy of Finland grants 285461 (H.T.), 330678 (H.T., J.R.), 277194 (H.L.), and 290677 (S.M.). We acknowledge the European Synchrotron Radiation Facility (ESRF) for providing synchrotron access for crystal data collection. We thank Prof. Janne Ihalainen (University of Jyväskylä) for all the help in all aspects of the paper, Prof. Gerrit Groenhof (University of Jyväskylä) for support, and Prof. Nikolai V. Tkachenko (Tampere University) for help and facilities for time-resolved absorption spectroscopy. We also thank M.Sc. Alli Liukkonen (University of Jyväskylä) and Dr. Heikki Häkkänen (University of Jyväskylä) for the assistance in laboratory …

fytokromitphytochrome structureProtein ConformationPhytochrome structureSpectral responsesspektroskopiafotobiologiabakteeritBacterial ProteinsHistidinePhysical and Theoretical ChemistryBinding Sites221 Nanotechnologyspectral responsesWaterBiliverdin protonationsäteilyWater networkkidetiedewater networkTyrosine1182 Biochemistry cell and molecular biologyPhytochromeDeinococcusproteiinitvalokemiabiliverdin protonationvalo
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Conversion of biliverdin to bilirubin by biliverdin reductase contributes to endothelial cell protection by heme oxygenase-1—evidence for direct and …

2009

Heme oxygenase-1 (HO-1) is highly protective in various pathophysiological states such as cardiovascular and neurodegenerative diseases. HO-1-derived bilirubin is an efficient scavenger of reactive oxygen and nitrogen species (RONS). It remains to determine whether conversion of biliverdin to bilirubin is an essential step for HO-1-conferred protection of endothelial cells. RONS scavenging activities of biliverdin versus bilirubin were assessed by different RONS generating systems and detection techniques. We also silenced the biliverdin reductase (BVR) or HO-1 gene in cultured primary human endothelial cells (HUVECs) and measured the effect on RONS formation upon stimulation with lipopolys…

LipopolysaccharidesOxidoreductases Acting on CH-CH Group DonorsUmbilical VeinsXanthine OxidaseNeutrophilsBilirubinNitrosationModels BiologicalAntioxidantschemistry.chemical_compoundPeroxynitrous AcidLeukocytespolycyclic compoundsHumansGene SilencingMolecular BiologyHemeReactive nitrogen speciesRespiratory BurstBiliverdinAngiotensin IIBiliverdineBiliverdin reductaseEndothelial CellsBilirubinFree Radical ScavengersAngiotensin IIMitochondriaEndothelial stem cellHeme oxygenasechemistryBiochemistryCytoprotectionGene Knockdown TechniquesTyrosineReactive Oxygen SpeciesCardiology and Cardiovascular MedicineHeme Oxygenase-1Journal of Molecular and Cellular Cardiology
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The hairpin extension controls solvent access to the chromophore binding pocket in a bacterial phytochrome: a UV-vis absorption spectroscopy study.

2021

AbstractSolvent access to the protein interior plays an important role in the function of many proteins. Phytochromes contain a specific structural feature, a hairpin extension that appears to relay structural information from the chromophore to the rest of the protein. The extension interacts with amino acids near the chromophore, and hence shields the chromophore from the surrounding solvent. We envision that the detachment of the extension from the protein surface allows solvent exchange reactions in the vicinity of the chromophore. This can facilitate for example, proton transfer processes between solvent and the protein interior. To test this hypothesis, the kinetics of the protonation…

Models MolecularProtein ConformationProtonation010402 general chemistryPhotochemistry01 natural sciencespH jump03 medical and health scienceschemistry.chemical_compoundPhytochrome ADeprotonationBacterial ProteinsPhotostationary statePhysical and Theoretical Chemistrychromophore protein systems030304 developmental biology0303 health sciencesBiliverdinBinding SitesPhytochromeProtein dynamicsBiliverdineconformational substatesChromophoreHydrogen-Ion Concentrationsolvent gating0104 chemical sciencesKineticschemistryprotein dynamicsSolventsSpectrophotometry UltravioletproteiinitvalokemiaDeinococcusPhytochromeProtonsPhotochemicalphotobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology
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Human Biliverdin Reductase Suppresses Goodpasture Antigen-binding Protein (GPBP) Kinase Activity

2010

The Ser/Thr/Tyr kinase activity of human biliverdin reductase (hBVR) and the expression of Goodpasture antigen-binding protein (GPBP), a nonconventional Ser/Thr kinase for the type IV collagen of basement membrane, are regulated by tumor necrosis factor (TNF-α). The pro-inflammatory cytokine stimulates kinase activity of hBVR and activates NF-κB, a transcriptional regulator of GPBP mRNA. Increased GPBP activity is associated with several autoimmune conditions, including Goodpasture syndrome. Here we show that in HEK293A cells hBVR binds to GPBP and down-regulates its TNF-α-stimulated kinase activity; this was not due to a decrease in GPBP expression. Findings with small interfering RNA to h…

Small interfering RNAKinaseBiliverdin reductaseNF-κBCell BiologyBiologyBiochemistryMolecular biologyType IV collagenchemistry.chemical_compoundchemistryTranscriptional regulationKinase activitySignal transductionMolecular BiologyJournal of Biological Chemistry
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Glutathionyl-biliverdin IXα, a new heme catabolite in a marine annelid: Sex and cell specific accumulation.

2011

Abstract We have isolated and characterized the green pigment accumulating in coelomic cells (eleocytes) of the common clam worm Nereis virens by means of RP-HPLC and ESI-tandem mass spectrometry. This pigment is a novel biliverdin-glutathione conjugate in which the glutathione is linked to the biliverdin-backbone via a thioether bond. The yolk precursor vitellogenin, a female-specific high-density lipoprotein ( ρ  = 1179 kg/m 3 ) with a native molecular mass of ∼500 kDa and a subunit mass of ∼150 kDa, is capable of transporting this pigment as well as heme. The sex-independent large discoidal lipoprotein present in the coelomic fluid, which is sequestered by the eleocytes, could also be sh…

Malefood.ingredientProtein subunitHemeBiochemistrychemistry.chemical_compoundVitellogeninfoodYolkAnimalsHemeSex CharacteristicsBiliverdinMolecular massbiologyBiliverdinePolychaetaGeneral MedicineGlutathioneGlutathionechemistryBiochemistrybiology.proteinlipids (amino acids peptides and proteins)FemaleHemoglobinBiochimie
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Inhibition of the mutagenicity of 2-nitrofluorene, 3-nitrofluoranthene and 1-nitropyrene by vitamins, porphyrins and related compounds, and vegetable…

1997

When 21 vitamins including related compounds haemin, chlorophyllin, chlorophyll, biliverdin and bilirubin, as well as juices from five fruits and 25 vegetables and solvent extracts from the residues of fruits and vegetables were tested for their antimutagenic potencies with respect to mutagenicity induced by 2-nitrofluorene (2-NF), 3-nitrofluoranthene (3-NFA) and 1-nitropyrene(1-NP) in Salmonella typhimurium TA98 the following results were obtained. The tetracyclic nitroarenes 3-NFA and 1-NP were in general more effectively antagonized by potent antimutagenic compounds than the tricyclic 2-NF. beta-Carotene, retinol, retinal, retinoic acid, retinol palmitate, riboflavin 5'-phosphate, alpha-…

Salmonella typhimuriumPorphyrinsBilirubinMutagenToxicologymedicine.disease_causechemistry.chemical_compoundbeta-CaroteneVegetablesmedicineFood scienceCarotenoidchemistry.chemical_classificationFluorenesPyrenesBiliverdinMutagenicity TestsChlorophyllinfood and beveragesAntimutagenic AgentsVitaminsGeneral MedicinechemistryBiochemistryAntimutagenic AgentsFruitSolventsAntimutagenMutagensFood ScienceFood and Chemical Toxicology
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Transient IR spectroscopy identifies key interactions and unravels new intermediates in the photocycle of a bacterial phytochrome.

2020

Phytochromes are photosensory proteins in plants, fungi, and bacteria, which detect red- and far-red light. They undergo a transition between the resting (Pr) and photoactivated (Pfr) states. In bacterial phytochromes, the Pr-to-Pfr transition is facilitated by two intermediate states, called Lumi-R and Meta-R. The molecular structures of the protein in these states are not known and the molecular mechanism of photoconversion is not understood. Here, we apply transient infrared absorption spectroscopy to study the photocycle of the wild-type and Y263F mutant of the phytochrome from Deinococcus radiodurans (DrBphP) from nanoto milliseconds. We identify two sequentially forming Lumi-R states …

Models MolecularLight Signal TransductionSpectrophotometry InfraredspektroskopiaMutantGeneral Physics and AstronomyInfrared spectroscopy010402 general chemistry01 natural sciences03 medical and health scienceschemistry.chemical_compoundProtein structureBacterial ProteinsinfrapunasäteilyPhysical and Theoretical ChemistryTyrosineSpectroscopy030304 developmental biology0303 health sciencesBiliverdinPhytochromebiologyChemistryDeinococcus radioduransbiology.organism_classification0104 chemical sciencesProtein Structure TertiaryMutationBiophysicsproteiinitvalokemiaDeinococcusPhytochromePhysical chemistry chemical physics : PCCP
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Fluorescence Properties of the Chromophore-Binding Domain of Bacteriophytochrome from Deinococcus radiodurans

2013

Fluorescent proteins are versatile tools for molecular imaging. In this study, we report a detailed analysis of the absorption and fluorescence properties of the chromophore-binding domain from Deinococcus radiodurans and its D207H mutant. Using single photon counting and transient absorption techniques, the average excited state lifetime of both studied systems was about 370 ps. The D207H mutation slightly changed the excited state decay profile but did not have a considerable effect on the average decay time of the system or the shape of the absorption and emission spectra of the biliverdin chromophore. We confirmed that the fluorescence properties of both samples are very similar in vivo…

Time FactorsFluorescence in the life sciencesPhotochemistrychemistry.chemical_compoundBimolecular fluorescence complementationBacterial ProteinsEscherichia coliMaterials ChemistryPhysical and Theoretical Chemistryta116BiliverdinbiologyPhytochromeBiliverdineta1182Deinococcus radioduransChromophorebiology.organism_classificationFluorescenceRecombinant ProteinsProtein Structure TertiarySurfaces Coatings and FilmschemistryMutationQuantum TheorySpectrophotometry UltravioletDeinococcusBinding domainThe Journal of Physical Chemistry B
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