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The resonances of the aromatic rings in the 1H NMR spectra at 360 MHz of ferrocytochrome c-552 of Euglena gracilis were investigated by double resonance techniques. The spin systems of the two tryptophan and four of the tyrosine residues could be identified. This analysis of the aromatic region of the 1H NMR spectrum provided evidence that His-14 is bound to the heme iron. It gave also some insight into the molecular dynamics of ferrocytochrome c-552 in that it showed that of the six aromatic rings, four tyrosines were rotating rapidly about the Cbeta-Cgamma bond, while one tyrosine and the single phenylalanine were restricted in their rotational mobilities by their environmnent in the protein.
R M Keller, and
K Wüthrich
May 1974,
The Biochemical journal,
R M Keller, and
K Wüthrich
May 1981,
Molecular and cellular biology,
R M Keller, and
K Wüthrich
February 1973,
Nature,
R M Keller, and
K Wüthrich
December 1988,
Biochemical and biophysical research communications,
R M Keller, and
K Wüthrich
February 1973,
Nature,
R M Keller, and
K Wüthrich
April 1992,
European journal of biochemistry,
R M Keller, and
K Wüthrich
May 1975,
FEBS letters,
R M Keller, and
K Wüthrich
January 1979,
FEBS letters,
R M Keller, and
K Wüthrich
August 1982,
The Journal of biological chemistry,
R M Keller, and
K Wüthrich
September 1977,
Biophysics of structure and mechanism,
