An electronically enhanced chiral sum frequency generation vibrational spectroscopy study of lipid-bound cytochrome c.
Electronically enhanced chiral SFG spectroscopy was employed to study the lipid bound cyt c in situ. It was directly observed that upon interacting with anionic phospholipids, the amino acid residues around the heme adopted the β-sheet conformation. In addition, the orientation of this newly formed β-sheet structure was found to be sensitive to the bulk pH.
School of Chemical Engineering, The University of Queensland, Brisbane, QLD 4072, Australia. k.nguyen9@uq.edu.au.
Khoi Tan
KT
Nguyen
D000818:Animals; D002417:Cattle; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008055:Lipids / Q000737:chemistry*; D010715:Phosphatidylglycerols / Q000737:chemistry; D017433:Protein Structure, Secondary; D013059:Spectrum Analysis, Raman
D008055:Lipids; D010715:Phosphatidylglycerols; D045304:Cytochromes c; C030345:1,2-dipalmitoylphosphatidylglycerol