Relaxation of solvent protons and deuterons by protein-bound Mn²⁺ ions. Theory and experiment for Mn²⁺-concanavalin A

Abstract

Despite the demonstrated utility of measurements of the magnetic field dependence of the magnetic relaxation rates of solvent protons in solutions of metalloproteins as an indicator of biochemical changes, it is becoming increasingly evident that quantitative comparisons of such data with the theory of relaxation, limited by the approximations and assumptions usually made, yield results for the strength of the solvent-paramagnetic ion interaction that generally do not make chemical sense. These results, when expressed as the number of solvent-donated ligands of the ions, usually give too large a value, typically by about twofold. It has been suggested by several investigators that a comparison of proton and deuteron relaxation rates could resolve the problem. Data are presented for the longitudinal relaxation rates of solvent protons and deuterons over more than four decades of magnetic field (from 0.01 to 270 MHz proton Larmor frequency) for solutions of Mn2+-concanavalin A, a protein for which the physical biochemistry is thoroughly documented, one that should be particularly tractable for such comparisons. The main conclusion is that, in the general case, there is no decade of magnetic field over which the mathematical criterion of best agreement of data with theory can be relied upon to yield quantitatively correct biochemical results; rather, biochemistry must still be a guide for elucidating relaxation pathways. © 1985.