High‐pressure 1H NMR study of pressure‐induced structural changes in the heme environments of metcyanomyoglobins

• Published in: Protein science Vol. 12; no. 2; pp. 207 - 217
• Main Authors: Kitahara, Ryo, Kato, Minoru, Taniguchi, Yoshihiro
• Format: Journal Article
• Language: English
• Published: Bristol Cold Spring Harbor Laboratory Press 01.02.2003
• Subjects: Animals; compressibility; DQF‐COSY, double‐quantum‐filtered correlation spectroscopy; Heme - chemistry; Heme - metabolism; HH, horse heart; Horses; Kinetics; Magnetic Resonance Spectroscopy; Mb, myoglobin; MbCN, metcyanomyoglobin; Metmyoglobin - chemistry; Metmyoglobin - metabolism; Models, Molecular; myoglobin; NMR; NMR, nuclear magnetic resonance; paramagnetic shift; Pressure; pressure effect; Protein Conformation; Protons; Structure-Activity Relationship; SW, sperm whale; Whales
• ISSN: 0961-8368; 1469-896X
• DOI: 10.1110/ps.4620103

The effect of pressure on the heme environment structure of sperm whale and horse heart metcyanomyoglobins was investigated up to 300 MPa by high‐pressure 1H NMR spectroscopy. Pressure‐induced changes in the distances between the observed protons and the heme iron atom were estimated from changes in the dipolar shift due to the paramagnetic effect on the protons. The changes showed that the heme peripheral structure as a whole was compressed by pressure; the movements of the protons in the heme peripheral residues were in the range of +0.16 to −0.54 Å/300 MPa. One‐dimensional compressibilities for the protons, excluding the protons of the distal His residue, were in the range of 1.0 × 10−4 to 6.1 × 10−4/MPa. The movements of the protons induced by pressure correlated well with the distance between the protons and cavities in the protein. The distal His residue (His 64) moved toward the outside of the heme pocket, but remained in the pocket even at 300 MPa. This movement was driven dominantly by a change in the dihedral angle around the Cα–Cβ rotational bond of the residue. Comparative work on horse heart metcyanomyoglobin implied that the conformational change of the His 64 imidazole ring was larger in the horse heart metcyanomyoglobin than in the sperm whale metcyanomyoglobin.