Ultrafast dynamics of ligands within heme proteins

Physiological bond formation and bond breaking events between proteins and ligands and their immediate consequences are difficult to synchronize and study in general. However, diatomic ligands can be photodissociated from heme, and thus in heme proteins ligand release and rebinding dynamics and traj...

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Bibliographic Details
Published in:Biochimica et biophysica acta 2008, Vol.1777 (1), p.15-31
Main Author: Vos, Marten H.
Format: Article
Language:English
Subjects:
Bacterial Proteins - metabolism
Carbon Monoxide - metabolism
Cytochrome
Cytochromes c - physiology
Electron Transport
Femtosecond spectroscopy
Guanylate Cyclase - physiology
Heme proteins
Heme-based sensors
Hemeproteins - chemistry
Hemeproteins - metabolism
Ligands
Molecular dynamics
Myoglobin - chemistry
Nitric Oxide - metabolism
Nitric Oxide Synthase - physiology
Oxidases
Temperature
Vibration
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Summary:Physiological bond formation and bond breaking events between proteins and ligands and their immediate consequences are difficult to synchronize and study in general. However, diatomic ligands can be photodissociated from heme, and thus in heme proteins ligand release and rebinding dynamics and trajectories have been studied on timescales of the internal vibrations of the protein that drive many biochemical reactions, and longer. The rapidly expanding number of characterized heme proteins involved in a large variety of functions allows comparative dynamics–structure–function studies. In this review, an overview is given of recent progress in this field, and in particular on initial sensing processes in signaling proteins, and on ligand and electron transfer dynamics in oxidases and cytochromes.
ISSN:0005-2728
0006-3002
0304-4173
1879-2650
DOI:10.1016/j.bbabio.2007.10.004