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In heme-based sensor proteins, ligand binding to heme in a sensor domain induces conformational changes that eventually lead to changes in enzymatic activity of an associated catalytic domain. The bacterial oxygen sensor FixL is the best-studied example of these proteins and displays marked differences in dynamic behavior with respect to model globin proteins. We report a mid-IR study of the configuration and ultrafast dynamics of CO in the distal heme pocket site of the sensor PAS domain FixLH, employing a recently developed method that provides a unique combination of high spectral resolution and range and high sensitivity. Anisotropy measurements indicate that CO rotates toward the heme plane upon dissociation, as is the case in globins. Remarkably, CO bound to the heme iron is tilted by ∼30° with respect to the heme normal, which contrasts to the situation in myoglobin and in present FixLH–CO X-ray crystal structure models. This implies protein-environment-induced strain on the ligand, which is possib...
| Authors: | Patrick Nuernberger; Kevin F. Lee; Adeline Bonvalet; Latifa Bouzhir-Sima; Jean-Christophe Lambry; Ursula Liebl; Manuel Joffre; Marten H. Vos | |
| Journal: | Journal of the American Chemical Society | |
| Year: | 2011 | |
| DOI: | 10.1021/ja204549n | |
| Publication date: | 07-10-2011 |
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