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 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.
Vos
Marten H
MH
Laboratoire d'Optique et Biosciences, CNRS, Ecole Polytechnique, F-91128 Palaiseau, France. marten.vos@polytechnique.edu
D001426:Bacterial Proteins / Q000378:metabolism; D002248:Carbon Monoxide / Q000378:metabolism; D045304:Cytochromes c / Q000502:physiology; D004579:Electron Transport; D006162:Guanylate Cyclase / Q000502:physiology; D006420:Hemeproteins / Q000737:chemistry / Q000378:metabolism*; D000071677:Histidine Kinase; D008024:Ligands; D009211:Myoglobin / Q000737:chemistry; D009569:Nitric Oxide / Q000378:metabolism; D019001:Nitric Oxide Synthase / Q000502:physiology; D013696:Temperature; D014732:Vibration
D001426:Bacterial Proteins; D006420:Hemeproteins; D008024:Ligands; D009211:Myoglobin; D009569:Nitric Oxide; D002248:Carbon Monoxide; D045304:Cytochromes c; D019001:Nitric Oxide Synthase; C067929:FixL protein, Bacteria; D000071677:Histidine Kinase; D006162:Guanylate Cyclase