Water may inhibit oxygen binding in hemoprotein models.

Abstract

Three distal imidazole pickets in a cytochrome c oxidase (CcO) model form a pocket hosting a cluster of water molecules. The cluster makes the ferrous heme low spin, and consequently the O(2) binding slow. The nature of the rigid proximal imidazole tail favors a high spin/low spin cross-over. The O(2) binding rate is enhanced either by removing the water, increasing the hydrophobicity of the gas binding pocket, or inserting a metal ion that coordinates to the 3 distal imidazole pickets.