The transfer of CO from heme a3 to the CuB site in Cytochrome c oxidase (CcO) after photolysis is studied using molecular dynamics simulations using an explicitly reactive, parametrized potential energy surface based on density functional theory calculations. After photodissociation from the heme-Fe, the CO ligand rebinds to the CuB site on the sub-picosecond time scale. Depending on the simulation protocol the characteristic time ranges from 260 fs to 380 fs which compares with an estimated 450 fs from experiment based on the analysis of the spectral changes as a function of time delay after the photodissociating pulse. Following photoexcitation ≈90% of the ligands are found to rebind to either the CuB (major component, 85%) or the heme-Fe (minor component, 2%) whereas about 10% remain in an unbound state. The infrared spectra of unbound CO in the active site is broad and featureless and no appreciable shift relative to gas-phase CO is found, which is in contrast to the situation in myoglobin. These observations explain why experimentally, unbound CO in the binuclear site of CcO has not been found as yet.
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14 April 2014
Research Article|
April 08 2014
CO-dynamics in the active site of cytochrome c oxidase
Maksym Soloviov;
Maksym Soloviov
Department of Chemistry,
University of Basel
, Klingelbergstrasse 80, 4056 Basel, Switzerland
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Markus Meuwly
Markus Meuwly
a)
Department of Chemistry,
University of Basel
, Klingelbergstrasse 80, 4056 Basel, Switzerland
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a)
Author to whom correspondence should be addressed. Electronic mail: m.meuwly@unibas.ch
J. Chem. Phys. 140, 145101 (2014)
Article history
Received:
January 20 2014
Accepted:
March 21 2014
Citation
Maksym Soloviov, Markus Meuwly; CO-dynamics in the active site of cytochrome c oxidase. J. Chem. Phys. 14 April 2014; 140 (14): 145101. https://doi.org/10.1063/1.4870264
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