skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Solution deuterium NMR quadrupolar relaxation study of heme mobility in myoglobin

Journal Article · · Journal of the American Chemical Society; (USA)
DOI:https://doi.org/10.1021/ja00184a013· OSTI ID:5092844

NMR spectroscopy has been used to monitor the quadrupolar relaxation and motional dynamics of {sup 2}H selectively incorporated into skeletal and side chain positions of the heme in sperm whale myoglobin. The hyperfine shifts of the heme resonances in paramagnetic states of myoglobin allow resolution of the signals of interest, and paramagnetic contributions to the observed line widths are shown to be insignificant. The {sup 2}H line widths for the skeletal positions of deuterohemin-reconstituted myoglobin yield a correlation time identical with that of overall protein tumbling (9 ns at 30{degree}C) and hence reflect an immobile heme group. The {sup 2}H NMR line widths of heme methyl groups exhibit motional narrowing indicative of very rapid internal rotation. Hence the methyl rotation is effectively decoupled from the overall protein tumbling, and the residual quadrupolar line width can be used directly to determine the protein tumbling rate. The {sup 2}H NMR lines from heme vinyl groups were found narrower than those from the heme skeleton. However, the range of quadrupolar coupling constants for sp{sup 2} hybridized C-{sup 2}H bonds does not permit an unequivocal interpretation in terms of mobility. 48 refs., 4 figs.

OSTI ID:
5092844
Journal Information:
Journal of the American Chemical Society; (USA), Vol. 111:2; ISSN 0002-7863
Country of Publication:
United States
Language:
English