Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity
Само за регистроване кориснике
2021
Аутори
Gligorijević, NikolaMinić, Simeon L.
Radibratović, Milica
Papadimitriou, Vassiliki
Nedić, Olgica
Sotiroudis, Theodore G.
Nikolić, Milan
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
Phycocyanobilin 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 acti...vity (~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.
Кључне речи:
Activity / Binding / Catalase / Phycocyanobilin / StructureИзвор:
Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 2021, 251, 119483-Издавач:
- Elsevier
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200168 (Универзитет у Београду, Хемијски факултет) (RS-MESTD-inst-2020-200168)
DOI: 10.1016/j.saa.2021.119483
ISSN: 1386-1425
WoS: 000621417500002
Scopus: 2-s2.0-85099780517
URI
https://www.sciencedirect.com/science/article/pii/S1386142521000597https://cherry.chem.bg.ac.rs/handle/123456789/4486
Колекције
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Gligorijević, Nikola AU - Minić, Simeon L. AU - Radibratović, Milica AU - Papadimitriou, Vassiliki AU - Nedić, Olgica AU - Sotiroudis, Theodore G. AU - Nikolić, Milan PY - 2021 UR - https://www.sciencedirect.com/science/article/pii/S1386142521000597 UR - https://cherry.chem.bg.ac.rs/handle/123456789/4486 AB - Phycocyanobilin 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. PB - Elsevier T2 - Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy T2 - Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy T1 - Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity VL - 251 SP - 119483 DO - 10.1016/j.saa.2021.119483 ER -
@article{ author = "Gligorijević, Nikola and Minić, Simeon L. and Radibratović, Milica and Papadimitriou, Vassiliki and Nedić, Olgica and Sotiroudis, Theodore G. and Nikolić, Milan", year = "2021", abstract = "Phycocyanobilin 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.", publisher = "Elsevier", journal = "Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, Spectrochimica Acta Part A: Molecular and Biomolecular SpectroscopySpectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy", title = "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity", volume = "251", pages = "119483", doi = "10.1016/j.saa.2021.119483" }
Gligorijević, N., Minić, S. L., Radibratović, M., Papadimitriou, V., Nedić, O., Sotiroudis, T. G.,& Nikolić, M.. (2021). Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. in Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy Elsevier., 251, 119483. https://doi.org/10.1016/j.saa.2021.119483
Gligorijević N, Minić SL, Radibratović M, Papadimitriou V, Nedić O, Sotiroudis TG, Nikolić M. Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity. in Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy. 2021;251:119483. doi:10.1016/j.saa.2021.119483 .
Gligorijević, Nikola, Minić, Simeon L., Radibratović, Milica, Papadimitriou, Vassiliki, Nedić, Olgica, Sotiroudis, Theodore G., Nikolić, Milan, "Nutraceutical phycocyanobilin binding to catalase protects the pigment from oxidation without affecting catalytic activity" in Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 251 (2021):119483, https://doi.org/10.1016/j.saa.2021.119483 . .