Proton magnetic relaxation of water sorbed by methaemoglobin crystals
P. m. r. relaxation times ( T 1 and T 2 ) have been measured as a function of regain and temperature for water sorbed by lyophilized methaemoglobin. The purpose of the work was to gain information regarding the nature and extent of water binding by the protein molecules. The T 1 results are interpreted in terms of an exchange between the sixth ligand position of the Fe (III) and other adsorption sites on the protein. At high temperatures the relaxation rate at a given regain reaches a limiting value which allows the fraction of ferric ions hydrated to be calculated. Above 16% regain all the Fe (III) is hydrated. At 21 and 35% regains a maximum appears in the relaxation rate at about -46 °C indicating a contribution from a more mobile phase which produces a T 1 minimum at that temperature. The T 2 data are consistent with a model in which the main contribution to the transverse relaxation rate comes from a tightly bound fraction of the water with ω 0 Ƭ c ≫1. The temperature dependence of T 2 exhibits three different regions: ( a ) a low temperature region where lg T 2 ∝ T -1 ; ( b ) an intermediate region with a steeper increase of T 2 with temperature; and ( c ) a high temperature where T 2 levels off.