Phenylalanine stacking enhances the red fluorescence of biliverdin IXα on UV excitation in sandercyanin fluorescent protein

Yadav, K and Ghosh, S and Barak, A and Schaefer, W and Subramanian, R (2022) Phenylalanine stacking enhances the red fluorescence of biliverdin IXα on UV excitation in sandercyanin fluorescent protein. In: FEBS Letters .

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Abstract

Biliverdin IXα (BV) binds to several prokaryotic and eukaryotic proteins. How nature exploits the versatility of BV's properties is not fully understood. Unlike free BV, the Sandercyanin fluorescent protein bound to BV (SFP-BV) shows enhanced red fluorescence (675 nm) on excitation in the UV region (380 nm). Site-directed mutagenesis showed that the BV complex of two SFP variants, F55A and E79A, resulted in the loss of red fluorescence. Crystal structures of the complexes of these proteins with BV show the absence of stacking interactions of the F55 phenyl ring with BV. BV changes from ZZZssa conformation in the wild-type to ZZZsss conformation in the variants. In the nonfluorescent mutants, the lowest excited state is destabilized, resulting in nonradiative decay. © 2022 Federation of European Biochemical Societies

Item Type:	Journal Article
Publication:	FEBS Letters
Publisher:	John Wiley and Sons Inc
Additional Information:	The copyright for this article belongs to John Wiley and Sons Inc
Department/Centre:	Division of Chemical Sciences > Inorganic & Physical Chemistry
Date Deposited:	07 Feb 2022 12:03
Last Modified:	07 Feb 2022 12:03
URI:	http://eprints.iisc.ac.in/id/eprint/71184

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