Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba3-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study

Constantinos Koutsoupakis; Tewfik Soulimane; Constantinos Varotsis

doi:10.1074/jbc.M112.403600

Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba₃-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study

Constantinos Koutsoupakis
, Tewfik Soulimane
, Constantinos Varotsis

Cyprus University of Technology

Research output: Contribution to journal › Article › peer-review

Abstract

Background: Cytochrome c oxidase reduces O₂ to H₂O, a reaction coupled to proton translocation across the membrane. Results: Photolysis of CO from the mixed valence form of cytochrome ba₃-CO does not lead to a heme a₃³⁺-Cu_B ¹⁺-CO binuclear center. Conclusion: The absence of reverse electron transfer between hemes a₃ and b is shown. Significance: Unique thermodynamic and kinetic properties of cytochrome ba₃ oxidase are presented.

Original language	English
Pages (from-to)	37495-37507
Number of pages	13
Journal	Journal of Biological Chemistry
Volume	287
Issue number	44
DOIs	https://doi.org/10.1074/jbc.M112.403600
Publication status	Published - 26 Oct 2012

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Koutsoupakis, Constantinos ; Soulimane, Tewfik ; Varotsis, Constantinos. / Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba₃-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study. In: Journal of Biological Chemistry. 2012 ; Vol. 287, No. 44. pp. 37495-37507.

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title = "Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba3-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study",

abstract = "Background: Cytochrome c oxidase reduces O2 to H2O, a reaction coupled to proton translocation across the membrane. Results: Photolysis of CO from the mixed valence form of cytochrome ba3-CO does not lead to a heme a33+-CuB 1+-CO binuclear center. Conclusion: The absence of reverse electron transfer between hemes a3 and b is shown. Significance: Unique thermodynamic and kinetic properties of cytochrome ba3 oxidase are presented.",

author = "Constantinos Koutsoupakis and Tewfik Soulimane and Constantinos Varotsis",

year = "2012",

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Koutsoupakis, C, Soulimane, T & Varotsis, C 2012, 'Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba₃-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study', Journal of Biological Chemistry, vol. 287, no. 44, pp. 37495-37507. https://doi.org/10.1074/jbc.M112.403600

Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba₃-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study. / Koutsoupakis, Constantinos; Soulimane, Tewfik; Varotsis, Constantinos.
In: Journal of Biological Chemistry, Vol. 287, No. 44, 26.10.2012, p. 37495-37507.

Research output: Contribution to journal › Article › peer-review

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T1 - Spectroscopic and kinetic investigation of the fully reduced and mixed valence states of ba3-cytochrome c oxidase from thermus thermophilus a fourier transform infrared (FTIR) and time-resolved step-scan FTIR study

AU - Koutsoupakis, Constantinos

AU - Soulimane, Tewfik

AU - Varotsis, Constantinos

PY - 2012/10/26

Y1 - 2012/10/26

N2 - Background: Cytochrome c oxidase reduces O2 to H2O, a reaction coupled to proton translocation across the membrane. Results: Photolysis of CO from the mixed valence form of cytochrome ba3-CO does not lead to a heme a33+-CuB 1+-CO binuclear center. Conclusion: The absence of reverse electron transfer between hemes a3 and b is shown. Significance: Unique thermodynamic and kinetic properties of cytochrome ba3 oxidase are presented.

AB - Background: Cytochrome c oxidase reduces O2 to H2O, a reaction coupled to proton translocation across the membrane. Results: Photolysis of CO from the mixed valence form of cytochrome ba3-CO does not lead to a heme a33+-CuB 1+-CO binuclear center. Conclusion: The absence of reverse electron transfer between hemes a3 and b is shown. Significance: Unique thermodynamic and kinetic properties of cytochrome ba3 oxidase are presented.

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JO - Journal of Biological Chemistry

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