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Τίτλος: Nanosecond ligand migration and functional protein relaxation in ba3 oxidoreductase: Structures of the B0, B1 and B2 intermediate states
Συγγραφείς: Nicolaides, Antonis 
Soulimane, Tewfik 
Varotsis, Constantinos 
metadata.dc.contributor.other: Νικολαϊδης, Αντώνης
Βαρώτσης, Κωνσταντίνος
Major Field of Science: Natural Sciences
Field Category: Earth and Related Environmental Sciences
Λέξεις-κλειδιά: Cytochrome c oxidase;Dynamics;Time-resolved step-scan FTIR
Ημερομηνία Έκδοσης: 1-Σεπ-2016
Πηγή: Biochimica et Biophysica Acta - Bioenergetics, 2016, vol. 1857, no. 9, pp. 1534-1540
Volume: 1857
Issue: 9
Start page: 1534
End page: 1540
Περιοδικό: Biochimica et Biophysica Acta - Bioenergetics 
Περίληψη: Nanosecond time-resolved step-scan FTIR spectroscopy (nTRS 2 -FTIR) has been applied to literally probe the active site of the carbon monoxide (CO)-bound thermophilic ba3 heme-copper oxidoreductase as it executes its function. The nTRS 2 - snapshots of the photolysed heme a3 Fe-CO/CuB species captured a "transition state" whose side chains prevent the photolysed CO to enter the docking cavity. There are three sets of ba3 photoproduct bands of docked CO with different orientation exhibiting different kinetics. The trajectories of the "docked" CO at 2122, 2129 and 2137 cm- 1 is referred to in the literature as B2, B1 and B0 intermediate states, respectively. The present data provided direct evidence for the role of water in controlling ligand orientation in an intracavity protein environment.
URI: https://hdl.handle.net/20.500.14279/9373
ISSN: 18792650
DOI: 10.1016/j.bbabio.2016.05.002
Rights: © Elsevier
Type: Article
Affiliation: Cyprus University of Technology 
University of Limerick 
Publication Type: Peer Reviewed
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