Solid-State Nitrogen-15 Nuclear Magnetic Resonance Study of the Schiff Base in Bacteriorhodopsin

Gerard S. Harbison, Judith Herzfeld, Robert G. Griffin

Research output: Contribution to journalArticle

100 Citations (Scopus)

Abstract

Solid-state 15N NMR has been employed to examine protonation of the Schiff base linkage in ϵ-[15N]lysylbacteriorhodopsin, the single protein in purple membrane. It is shown with spectra of model compounds that protonation of a Schiff base results in an approximate 150-ppm change in the isotropic 15N chemical shift. Concurrently, the breadth of the shift anisotropy decreases by a factor of about two from 600 to 270 ppm. The isotropic shift of the Schiff base linkage observed in dark-adapted ϵ-[15N]lysylbacteriorhodopsin closely matches those observed for the protonated model compounds, particularly the more weakly hydrogen-bonded ones. It also seems to be affected slightly by isomerization of the retinal.

Original languageEnglish (US)
Pages (from-to)1-5
Number of pages5
JournalBiochemistry
Volume22
Issue number1
DOIs
StatePublished - Jan 4 1983

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Bacteriorhodopsins
Schiff Bases
Magnetic Resonance Spectroscopy
Nitrogen
Protonation
Nuclear magnetic resonance
Purple Membrane
Anisotropy
Chemical shift
Isomerization
Hydrogen
Membranes
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Solid-State Nitrogen-15 Nuclear Magnetic Resonance Study of the Schiff Base in Bacteriorhodopsin. / Harbison, Gerard S.; Herzfeld, Judith; Griffin, Robert G.

In: Biochemistry, Vol. 22, No. 1, 04.01.1983, p. 1-5.

Research output: Contribution to journalArticle

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