Document Type
Article
Publication Date
12-2-2017
Publication Title
Biochemical and Biophysical Research Communications
Abstract
© 2017 Elsevier Inc. Endothelial nitric oxide synthase (eNOS) is a membrane-anchored enzyme. To highlight the potential role and effect of membrane phospholipids on the structure and activity of eNOS, we have incorporated the recombinant oxygenase subunit of eNOS into lipid nanodiscs. Two different size distribution modes were detected by multi-angle dynamic light scattering both for empty nanodiscs, and nanodiscs-bound eNOSoxy. The calculated hydrodynamic diameter for mode 1 species was 9.0 nm for empty nanodiscs and 9.8 nm for nanodisc bound eNOSoxy. Spectroscopic Griess assay was used to measure the enzymatic activity. Remarkably, the specific activity of nanodisc-bound eNOSoxy is ∼65% lower than the activity of free enzyme. The data shows that the nano-membrane environment affects the catalytic properties of eNOS heme domain.
Repository Citation
AlTawallbeh, Ghaith; Haque, Mohammad M.; Streletzky, Kiril A.; Stuehr, Dennis J.; and Bayachou, Mekki, "Endothelial Nitric Oxide Synthase Oxygenase on Lipid Nanodiscs: A Nano-Assembly Reflecting Native-Like Function of eNOS" (2017). Physics Faculty Publications. 416.
https://engagedscholarship.csuohio.edu/sciphysics_facpub/416
DOI
10.1016/j.bbrc.2017.09.131
Version
Postprint
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Volume
493
Issue
4
