Spectrochim Acta A Mol Biomol Spectrosc
December 2024
A study on the absorption and fluorescence properties of the 8-anilino-1-naphthalenesulfonate (ANS) fluorescent probe was performed in order to (i) verify the validity of its classification as hydrophobic probe and (ii) to assess the reliability of the interpretation of the ANS fluorescence enhancement upon protein binding as the evidence for the existence of hydrophobic binding sites on the protein molecules. We observed an enhancement of the ANS fluorescence in hydrophilic media: DMSO, polyethylene glycol (PEG400) and glycerol to the values characteristic of ANS complexes with globular proteins, and all ANS fluorescence characteristics (except anisotropy) in PEG400 and in complex with bovine serum albumin are identical. We observed an increase in the ANS fluorescence with a nonzero anisotropy in an aqueous medium in the presence of an amphiphilic cetyltrimethylammonium cation as a result of the formation of the 1:1 complex with ANS.
View Article and Find Full Text PDFCytochrome (CytC), a one-electron carrier, transfers electrons from complex to cytochrome oxidase (CcO) in the electron-transport chain. Electrostatic interaction with the partners, complex and CcO, is ensured by a lysine cluster near the heme forming the Universal Binding Site (UBS). We constructed three mutant variants of mitochondrial CytC with one (2Mut), four (5Mut), and five (8Mut) Lys->Glu substitutions in the UBS and some compensating Glu->Lys substitutions at the periphery of the UBS for charge compensation.
View Article and Find Full Text PDFNeuroglobin (Ngb) is a cytosolic heme protein that plays an important role in protecting cells from apoptosis through interaction with oxidized cytochrome (Cyt ) released from mitochondria. The interaction of reduced Ngb and oxidized Cyt is accompanied by electron transfer between them and the reduction in Cyt . Despite the growing number of studies on Ngb, the mechanism of interaction between Ngb and Cyt is still unclear.
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