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Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/493

Title: Ultrafast electron transfer in riboflavin binding protein in macromolecular crowding of nano-sized micelle
Authors: Rakshit, Surajit
Saha, Ranajay
Verma, Pramod Kumar
Mitra, Rajib Kumar
Pal, Samir Kumar
Keywords: Molecular and macromolecular crowding
Electron transfer in riboflavin binding protein in cellular environments
Picosecond-resolved electron transfer dynamics of Vitamin B2 in protein
Ligand binding in micellar crowding
Tertiary structure of riboflavin binding protein
Issue Date: 2012
Publisher: Biochimie
Citation: Surajit Rakshit, Ranajay Saha, Pramod Kumar Verma, Rajib Kumar Mitra, Samir Kumar Pal, Ultrafast electron transfer in riboflavin binding protein in macromolecular crowding of nano-sized micelle, Biochimie, 2012, 94(12), 2673-2680
Abstract: In this contribution, we have studied the dynamics of electron transfer (ET) of a flavoprotein to the bound cofactor, an important metabolic process, in a model molecular/macromolecular crowding environments. Vitamin B2 (riboflavin, Rf) and riboflavin binding protein (RBP) are used as model cofactor and flavoprotein,respectively. An anionic surfactant sodium dodecyl sulfate (SDS) is considered to be model crowding agent. A systematic study on the ET dynamics in various SDS concentration, ranging from below critical micellar concentration (CMC), where the surfactants remain as monomeric form to above CMC, where the surfactants self-assemble to form nanoscopic micelle, explores the dynamics of ET in the model molecular and macromolecular crowding environments. With energy selective excitation in picosecond-resolved studies, we have followed temporal quenching of the tryptophan residue of the protein and Rf in the RBP-Rf complex in various degrees of molecular/macromolecular crowding. The structural integrity of the protein (secondary and tertiary structures) and the vitamin binding capacity of RBP have been investigated using various techniques including UV-Vis, circular dichroism (CD) spectroscopy and dynamic light scattering (DLS) studies in the crowding environments. Our finding suggests that the effect of molecular/macromolecular crowding could have major implication in the intra-protein ET dynamics in cellular environments.
URI: http://hdl.handle.net/123456789/493
Appears in Collections:2012

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