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dc.creatorGligorijević, Nikola
dc.creatorMinić, Simeon
dc.creatorRadibratović, Milica
dc.creatorPapadimitriou, Vassiliki
dc.creatorNedić, Olgica
dc.creatorSotiroudis, Theodore G.
dc.creatorNikolić, Milan
dc.date.accessioned2021-02-11T15:04:39Z
dc.date.available2021-02-11T15:04:39Z
dc.date.issued2021
dc.identifier.issn1386-1425
dc.identifier.urihttps://cer.ihtm.bg.ac.rs/handle/123456789/4226
dc.description.abstractPhycocyanobilin is a dark blue linear tetrapyrrole chromophore covalently attached to protein subunits of phycobiliproteins present in the light-harvesting complexes of the cyanobacteria Arthrospira platensis (Spirulina “superfood”). It shows exceptional health-promoting properties and emerging use in various fields of bioscience and industry. This study aims to examine the mutual impact of phycocyanobilin interactions with catalase, a life-essential antioxidant enzyme. Fluorescence quenching experiments demonstrated moderate binding (Ka of 3.9 × 104 M−1 at 25 °C; n = 0.89) (static type), while van't Hoff plot points to an enthalpically driven ligand binding (ΔG = −28.2 kJ mol−1; ΔH = −41.9 kJ mol−1). No significant changes in protein secondary structures (α-helix content ~22%) and thermal protein stability in terms of enzyme tetramer subunits (Tm ~ 64 °C) were detected upon ligand binding. Alterations in the tertiary catalase structure were found without adverse effects on enzyme activity (~2 × 106 IU/mL). The docking study results indicated that the ligand most likely binds to amino acid residues (Asn141, Arg 362, Tyr369 and Asn384) near the cavity between the enzyme homotetramer subunits not related to the active site. Finally, complex formation protects the pigment from free-radical induced oxidation (bleaching), suggesting possible prolongation of its half-life and bioactivity in vivo if bound to catalase.sr
dc.language.isoensr
dc.publisherElseviersr
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200168/RS//sr
dc.rightsrestrictedAccesssr
dc.sourceSpectrochimica Acta - Part A: Molecular and Biomolecular Spectroscopysr
dc.subjectPhycocyanobilinCatalaseBindingStructureActivitysr
dc.subjectPhycocyanobilinsr
dc.subjectCatalasesr
dc.subjectBindingsr
dc.subjectStructuresr
dc.subjectActivitysr
dc.titleNutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activitysr
dc.typearticlesr
dc.rights.licenseARRsr
dcterms.abstractПападимитриоу, Вассилики; Радибратовић, Милица; Минић, Симеон; Глигоријевић, Никола; Недић, Олгица; Сотироудис, Тхеодоре Г.; Николић, Милан;
dc.citation.volume251
dc.citation.spage119483
dc.citation.rankM21~
dc.identifier.pmid33515920
dc.identifier.doi10.1016/j.saa.2021.119483
dc.identifier.scopus2-s2.0-8509978051
dc.identifier.wos000621417500002
dc.type.versionpublishedVersionsr


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