PMID: 6615819Aug 16, 1983

High-pressure nuclear magnetic resonance studies of hemoproteins. Pressure-induced structural changes in the heme environments of ferric low-spin metmyoglobin complexes

I Morishima, M Hara


In order to gain an insight into nonbonded interactions in the heme microenvironments of hemoproteins, proton NMR spectra of the cyanide and methylamine complexes of metmyoglobin and its derivatives reconstituted with deutero- and meso-hemins in H2O were studied under high pressures. The exchangeable NH proton of distal histidyl imidazole exhibits substantial pressure-induced shift while the proximal histidyl NH proton shows no pressure effect for the cyanide complexes. The heme peripheral proton signals, especially 5- and 8-methyl and vinyl C alpha H resonances, were also affected by pressure. These observations are interpreted as arising from pressure-induced structural changes in the heme crevice in which the pressure effects are localized to the distal side rather than the proximal side and from possible changes in the van der Waals contacts at the heme periphery with nearby amino acid residues.


Jan 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·G B OgunmolaW Kauzmann
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Jul 1, 1969·Proceedings of the National Academy of Sciences of the United States of America·R G ShulmanM Brunori
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Jun 15, 2005·Biochimica Et Biophysica Acta·Céline BatailleSerge Pin
Sep 12, 1998·Biochimica Et Biophysica Acta·K Heremans, L Smeller
Oct 2, 2002·European Journal of Biochemistry·Camille LoupiacPatrick Calmettes
Mar 15, 2001·European Journal of Biochemistry·Y O KamatariL J Smith
Apr 25, 2013·Progress in Nuclear Magnetic Resonance Spectroscopy·Ryo KitaharaKazuyuki Akasaka
May 31, 1984·Biochemical and Biophysical Research Communications·I Morishima, M Hara
Aug 29, 2017·Critical Reviews in Food Science and Nutrition·K H BakV Orlien

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