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Biophys J, October 1999, p. 2153-2174, Vol. 77, No. 4
chovský,**Max Planck Institut für Molekulare Physiologie, Abteilung Physikalische Biochemie, 44227 Dortmund, Germany; #Biophysics Group, Los Alamos National Laboratory, Los Alamos, New Mexico 87545, USA; and §Biology Department, Brookhaven National Laboratory, Upton, New York 11973 USA
We have used x-ray crystallography to determine the
structures of sperm whale myoglobin (Mb) in four different ligation
states (unligated, ferric aquomet, oxygenated, and
carbonmonoxygenated) to a resolution of better than 1.2 Å. Data
collection and analysis were performed in as much the same way as
possible to reduce model bias in differences between structures. The
structural differences among the ligation states are much smaller than
previously estimated, with differences of <0.25 Å root-mean-square
deviation among all atoms. One structural parameter previously thought
to vary among the ligation states, the proximal histidine (His-93)
azimuthal angle, is nearly identical in all the ferrous complexes,
although the tilt of the proximal histidine is different in the
unligated form. There are significant differences, however, in the heme geometry, in the position of the heme in the pocket, and in the distal
histidine (His-64) conformations. In the CO complex the majority
conformation of ligand is at an angle of 18 ± 3° with respect
to the heme plane, with a geometry similar to that seen in encumbered
model compounds; this angle is significantly smaller than reported
previously by crystallographic studies on monoclinic Mb crystals, but
still significantly larger than observed by photoselection. The distal
histidine in unligated Mb and in the dioxygenated complex is best
described as having two conformations. Two similar conformations are
observed in MbCO, in addition to another conformation that has been
seen previously in low-pH structures where His-64 is doubly protonated.
We suggest that these conformations of the distal histidine correspond
to the different conformational substates of MbCO and MbO2
seen in vibrational spectra. Full-matrix refinement provides
uncertainty estimates of important structural parameters. Anisotropic
refinement yields information about correlated disorder of atoms; we
find that the proximal (F) helix and heme move approximately as rigid
bodies, but that the distal (E) helix does not.
Biophys J, October 1999, p. 2153-2174, Vol. 77, No. 4
© 1999 by the Biophysical Society 0006-3495/99/10/2153/22 $2.00
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