Affordable Access

Heme methyl hyperfine-shifted nuclear magnetic resonance peaks assigned by selective deuteration as indicators of heme-protein interactions in metmyoglobins.

Authors
Type
Published Article
Journal
Biochimica et Biophysica Acta
0006-3002
Publisher
Elsevier
Publication Date
Volume
622
Issue
2
Pages
210–218
Identifiers
PMID: 7378450
Source
Medline
License
Unknown

Abstract

The heme methyl resonances in a variety of high-spin, low-spin and spin-equilibrium forms of sperm whale metmyoglobin have been assigned by reconstituting myoglobin with selectively deuterated hemes. Two patterns for the heme methyl hyperfine shifts are observed, one characteristic of the low-spin state and the other typical of the high-spin state. The two protein forms which can change the position of their spin equilibrium significantly with changing temperature exhibit the pattern of the dominant spin state component at any temperature. The different hyperfine shift patterns for the low-spin and high-spin states are concluded to arise not from different heme-protein contacts in the two spin states, but from characteristic differential sensitivities of the dominant spin transfer mechanisms to the same rhombic perturbation.

Statistics

Seen <100 times