Ultrafast electron transfer in riboflavin binding protein in macromolecular crowding of nano-sized micelle.

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 B(2) (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.

journal_name

Biochimie

journal_title

Biochimie

authors

Rakshit S,Saha R,Verma PK,Mitra RK,Pal SK

doi

10.1016/j.biochi.2012.08.005

subject

Has Abstract

pub_date

2012-12-01 00:00:00

pages

2673-80

issue

12

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(12)00329-X

journal_volume

94

pub_type

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