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Biophysical Journal 33: 469-474 (1981)
© 1981 the Biophysical Society

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NMR relaxation of protein and water protons in methemoglobin solutions.

M Eisenstadt

ABSTRACT

Hemoglobin (Hb) proton spins rapidly equilibrate among themselves after an initial excitation, and relax toward thermal equilibrium as a unit. In the diamagnetic form, spin diffusion to nearby methyl relaxation sinks can account for this. For metHb, four strong heme relaxation centers dominate, and spin diffusion must occur over long distances. A sizeable difference in protein T1 is found between H2O and D2O solutions, much more than for diamagnetic Hb, consistent with internal H2O acting as a spin carrier to the heme.






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Copyright © 1981 by the Biophysical Society.