Structural dynamics and reactivity in hemoglobin.

Substantial new insights into the structural mechanism underlying the cooperative oxygen binding properties of hemoglobin have resulted from studies on non-equilibrium forms of hemoglobin using time resolved Raman, transient absorption and cryogenic trapping techniques. In this paper a review and a comparison of these related works is presented in an effort to develop a coherent and unified picture depicting the relationship between structural dynamics and function.