ISSN 1017-2548(Print)
ISSN 2234-8530(Online)
Volume 28, Number 1
JKCSEZ 28(1)
February 20, 1984 

The stability difference of metmyoglobin in H2O and D2O at pH 5.7 and pH 7.0 toward pressure denaturation is studied. Metmyoglobin is denatured in D2O at smaller pressure than in H2O. The stability difference in H2O and D2O is more pronounced at pH 5.7 than at pH 7. The main reasons for the stability difference in H2O and D2O are the difference in positive charge due to H+and D+ binding to the protein in H2O and D2O, and the structural change that accompany deuteration.