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Observation of Ligand Transfer in ba3 Oxidase from Thermus thermophilus: Simultaneous FTIR Detection of Photolabile Heme a32+–CN and Transient CuB2+–CN Complexes

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Department of Chemistry, University of Cyprus, P.O. Box 20537, 1678 Nicosia, Cyprus
Chemical and Environmental Sciences Department and Materials & Surface Science Institute, University of Limerick, Limerick, Ireland
Cite this: J. Phys. Chem. B 2012, 116, 30, 8955–8960
Publication Date (Web):July 5, 2012
https://doi.org/10.1021/jp305096y
Copyright © 2012 American Chemical Society

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    Abstract

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    FTIR and light-minus-dark FTIR spectroscopy have been employed to investigate the reaction of oxidized and fully reduced ba3 oxidase with cyanide. The characterization of the structures of the bound CN in the binuclear heme Fe–CuB center is essential, given that a central issue in the function of ba3 oxidase is the extent to which the partially reduced substrates interact with the two metals. In the reaction of oxidized ba3 oxidase with cyanide the initially formed heme a33+-C≡N–CuB2+ species with ν(CN) frequency at 2152 cm–1 was replaced by a photolabile complex with a frequency at 2075 cm–1 characteristic of heme a32+-CN. Photolysis of the heme a32+-CN adduct produced a band at 2146 cm–1 attributed to the formation of a transient CuB2+–CN complex. All forms are pH independent between pH 5.5–9.5 and at pD 7.5 indicating the absence of ionizable groups that influence the properties of the cyanide complexes. In contrast to previous reports, our results show that CN does not bind simultaneously to both heme a32+ and CuB2+ to form the mixed valence a32+-CN·CuB2+CN species. The photolysis products of the heme a32+-CN/CuB2+ and heme a32+-CN/CuB1+ species are different suggesting that relaxation dynamics in the binuclear center following ligand photodissociation are dependent on the oxidation state of CuB.

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    Cited By

    This article is cited by 5 publications.

    1. Antonis Nicolaides, Tewfik Soulimane, Constantinos Varotsis. Reversible temperature-dependent high- to low-spin transition in the heme Fe–Cu binuclear center of cytochrome ba 3 oxidase. RSC Advances 2019, 9 (9) , 4776-4780. https://doi.org/10.1039/C8RA09954E
    2. Antonis Nicolaides, Tewfik Soulimane, Constantinos Varotsis. ns-μs Time-Resolved Step-Scan FTIR of ba3 Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927. International Journal of Molecular Sciences 2016, 17 (10) , 1657. https://doi.org/10.3390/ijms17101657
    3. Antonis Nicolaides, Tewfik Soulimane, Constantinos Varotsis. Nanosecond ligand migration and functional protein relaxation in ba 3 oxidoreductase: Structures of the B 0 , B 1 and B 2 intermediate states. Biochimica et Biophysica Acta (BBA) - Bioenergetics 2016, 1857 (9) , 1534-1540. https://doi.org/10.1016/j.bbabio.2016.05.002
    4. Andreas Loullis, Mohamed Radzi Noor, Tewfik Soulimane, Eftychia Pinakoulaki. The structure of a ferrous heme-nitro species in the binuclear heme a 3 /Cu B center of ba 3 -cytochrome c oxidase as determined by resonance Raman spectroscopy. Chemical Communications 2015, 51 (2) , 286-289. https://doi.org/10.1039/C4CC08019J
    5. Antonis Nicolaides, Tewfik Soulimane, Constantinos Varotsis. Detection of functional hydrogen-bonded water molecules with protonated/deprotonated key carboxyl side chains in the respiratory enzyme ba 3 -oxidoreductase. Physical Chemistry Chemical Physics 2015, 17 (12) , 8113-8119. https://doi.org/10.1039/C5CP00043B

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