0000000000161362

AUTHOR

Maria Arbona

showing 2 related works from this author

Spectroscopic studies of water-soluble superstructured iron(III) porphyrin. Interaction with the bovine serum albumin protein

2018

Acid-base equilibrium of the “one-face”-hindered sulfonated porphyrin, α5,15-[2,2′(dodecamethyleneoxy),(5-sulfonato)diphenyl]-10,20-bis(2-hydroxy,5-sulfonatophenyl)porphyrinato iron(III), has been ...

biologyAlbumin02 engineering and technology010402 general chemistry021001 nanoscience & nanotechnology01 natural sciencesPorphyrin0104 chemical scienceslaw.inventionchemistry.chemical_compoundWater solublechemistrylawMaterials Chemistrybiology.proteinPhysical and Theoretical ChemistryBovine serum albumin0210 nano-technologyElectron paramagnetic resonanceNuclear chemistryJournal of Coordination Chemistry
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Protein Unfolding:1H-NMR Studies of Paramagnetic Ferricytochrome c-550 from Horse Heart

2005

Electronic transfer protein cytochrome c-550 from horse heart is studied in the unfolded state by means of paramagnetic 1H NMR. The protein contains 104 aminoacid residues and a heme group with low spin FeIII ion in the oxidized form of protein. The global secondary structure is of the α-helix type as occurs in the case of very other cytochromes c investigated such as cyt c-550 from Thiobacillus versutus or cyt c-551 from Pseudomonas aeruginosa. We have studied the coordination characteristic and electronic properties of heme iron horse heart ferricytochrome c-550 at increasing denaturing conditions (up to 3.1 M GuHCl and 288-323 K). The 1H T1 values of the signals were measured and some re…

chemistry.chemical_classificationCytochromebiologyLigandSpin transitionNuclear magnetic resonance spectroscopyInorganic Chemistrychemistry.chemical_compoundCrystallographychemistryProton NMRMetalloproteinbiology.proteinProtein secondary structureHemeZeitschrift für anorganische und allgemeine Chemie
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