Nanosecond ligand migration and functional protein relaxation in ba3 oxidoreductase: Structures of the B0, B1 and B2 intermediate states

Antonis Nicolaides; Tewfik Soulimane; Constantinos Varotsis

doi:10.1016/j.bbabio.2016.05.002

Nanosecond ligand migration and functional protein relaxation in ba₃ oxidoreductase: Structures of the B₀, B₁ and B₂ intermediate states

Antonis Nicolaides
, Tewfik Soulimane
, Constantinos Varotsis

Cyprus University of Technology

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

Abstract

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/Cu_B 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.

Original language	English
Pages (from-to)	1534-1540
Number of pages	7
Journal	Biochimica et Biophysica Acta - Bioenergetics
Volume	1857
Issue number	9
DOIs	https://doi.org/10.1016/j.bbabio.2016.05.002
Publication status	Published - 1 Sep 2016

Keywords

Cytochrome c oxidase
Dynamics
Time-resolved step-scan FTIR

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10.1016/j.bbabio.2016.05.002

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title = "Nanosecond ligand migration and functional protein relaxation in ba3 oxidoreductase: Structures of the B0, B1 and B2 intermediate states",

abstract = "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.",

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T2 - Structures of the B0, B1 and B2 intermediate states

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AU - Soulimane, Tewfik

AU - Varotsis, Constantinos

PY - 2016/9/1

Y1 - 2016/9/1

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AB - 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.

KW - Cytochrome c oxidase

KW - Dynamics

KW - Time-resolved step-scan FTIR

UR - https://www.scopus.com/pages/publications/84975275022

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JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

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ER -

Nanosecond ligand migration and functional protein relaxation in ba₃ oxidoreductase: Structures of the B₀, B₁ and B₂ intermediate states

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Keywords

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