1H-NMR spectra of deoxy myoglobins (Mbs) from shark (Galeorhinus japonicus), horse, and sperm whale have been studied to gain insights into their active site structure. It has been demonstrated for the first time that nuclear Overhauser effect (NOE) can be observed between heme peripheral side-chain proton resonances of these paramagnetic complexes. Val-E11 methyl and His-F8 C delta H proton resonances of these Mbs were also assigned from the characteristic shift and line width. The hyperfine shift of the former resonance was used to calculate the magnetic anisotropy of the protein. The shift analysis of the latter resonance, together with the previously assigned His-F8 N delta H proton resonance, revealed that the strain on the Fe-N epsilon bond is in the order horse Mb approximately whale Mb < shark Mb and that the hydrogen bond strength of the His-F8 N delta H proton to the main-chain carbonyl oxygen in the preceding turn of the F helix is in the order shark Mb < horse Mb < whale Mb. Weaker Feporphyrin interaction in shark Mb was manifested in a smaller shift of the heme methyl proton resonance and appears to result from distortion of the coordination geometry in this Mb. Larger strain on the Fe-N epsilon bond in shark Mb should be to some extent attributed to its lowered O2 affinity (P50 = 1.1 mmHg at 20 degrees C), compared to whale and horse Mbs.
Advanced Spaceborne Thermal Emission and Reflection Radiometer (ASTER), one of five sensors on Terra, has five bands (10 to 14) in the thermal infrared (TIR) region. These TIR bands are radiometrically calibrated by one onboard blackbody with the function of changing temperature between 270 and 340 K. In normal operation the blackbody is set up at 270 K, and a constant coefficient in a quadratic radiometric calibration equation for each detector is adjusted at that temperature before each Earth observation, but the gain coefficient cannot be adjusted at this time, while it can periodically be updated by long term calibration in which the blackbody is measured at 270, 300, 320, and 340 K. On the other hand the sensor response of all bands (particularly band 12) has been degrading since the launch, and periodical updating of the gain coefficient does not fully follow the degradation, so that the calibration error on level-1 (L1) products is often unacceptable. We therefore have developed a recalibration method which is easily applied to L1 products by a general user. By using this method, the calibration error will mostly be reduced below the level of NEDT.
The molecular structure of the active site of myoglobin from the shark, Galeorhinusjaponicus, has been studied by 'H-NMR. Some hyperfine-shifted amino acid proton resonances in the met-cyano form of G. japonicus myoglobin have been unambiguously assigned by the combined use of various two-dimensional NMR techniques; they were compared with the corresponding resonances in Physter catodon myoglobin. The orientations of ThrElO and IleFG.5 residues relative to the heme in G. japonicus met-cyano myoglobin were semiquantitatively estimated from the analysis of their shifts using the magnetic susceptibility tensor determined by a method called MATDUHM ( Mol. Biol. 153, 117-1241. In spite of a substantial difference in shift between the corresponding amino acid proton resonances for the two proteins, the orientations of these amino acid residues relative to the heme in the active site of both myoglobins were found to be highly alike.NMR of paramagnetic hemoproteins has provided a wealth of information about the structural properties of their active sites [l-61. 'H-NMR resonances arising from heme peripheral groups and amino acid residues near the heme have been effectively used as a useful structural probe in the NMR study of hemoprotein because these resonances are resolved well outside the poorly resolved diamagnetic envelope in the chemical shift region of 0 -10 ppm and they are quite sensitive to the heme molecular environments. Additionally, the observation of the nuclear Overhauser effect (NOE) [7], even in the presence of paramagnetic relaxation, allows not only the signal assignments of hyperfine-shifted resonances [3, 8 -101 but also the determination of internal mobility of specific groups in the heme pocket [ l l -141.As far as the structural determination of the active site in hemoprotein is concerned, resonances of non-coordinated amino acid protons are of particular importance because of their extremely high sensitivity to the spatial position of the nuclei relative to the heme [I5 -171. Their hyperfine shifts are purely pseudo-contact shifts (dPJ and hence can be interpreted quantitatively in terms of the dipolar interaction between Correspondence to Y. Yamamoto,
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