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Biophys J, April 2000, p. 2107-2115, Vol. 78, No. 4
Centro Brasileiro de Pesquisas Físicas, 22290-180 Rio de Janeiro, Brazil
Electron nuclear double resonance (ENDOR) spectroscopy
has been used to study protons in nitrosyl horse heart myoglobin
(MbNO). 1H ENDOR spectra were recorded for different
settings of the magnetic field. Detailed analysis of the ENDOR powder
spectra, using computer simulation, based on the
"orientation-selection" principle, leads to the identification of
the available protons in the heme pocket. We observe hyperfine
interactions of the N(HisF8)-Fe2+-N(NO) complex with five
protons in axial and with eight protons in the rhombic symmetry along
different orientations, including those of the principal axes of the
g-tensor. Protons from His-E7 and Val-E11 residues are
identified in the two symmetries, rhombic and axial, exhibited by MbNO.
Our results indicate that both residues are present inside the heme
pocket and help to stabilize one particular conformation.
Biophys J, April 2000, p. 2107-2115, Vol. 78, No. 4
© 2000 by the Biophysical Society 0006-3495/00/04/2107/09 $2.00
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