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Int. J. Mol. Sci. 2016, 17(10), 1657; doi:10.3390/ijms17101657

ns-μs Time-Resolved Step-Scan FTIR of ba3 Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927

1
Department of Environmental Science and Technology, Cyprus University of Technology, P.O. Box 50329, 3603 Lemesos, Cyprus
2
Chemical and Environmental Science Department and Materials & Surface Science Institute, University of Limerick, V94 T9PX Limerick, Ireland
*
Author to whom correspondence should be addressed.
Academic Editor: Samuel De Visser
Received: 15 August 2016 / Revised: 13 September 2016 / Accepted: 21 September 2016 / Published: 29 September 2016
(This article belongs to the Special Issue Computational Modelling of Enzymatic Reaction Mechanisms)
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Abstract

Time-resolved step-scan FTIR spectroscopy has been employed to probe the dynamics of the ba3 oxidoreductase from Thermus thermophilus in the ns-μs time range and in the pH/pD 6–9 range. The data revealed a pH/pD sensitivity of the D372 residue and of the ring-A propionate of heme a3. Based on the observed transient changes a model in which the protonic connectivity of w941-w946-927 to the D372 and the ring-A propionate of heme a3 is described. View Full-Text
Keywords: cytochrome ba3; ns time-resolved step-scan FTIR; heme-copper oxidoreductases cytochrome ba3; ns time-resolved step-scan FTIR; heme-copper oxidoreductases
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Nicolaides, A.; Soulimane, T.; Varotsis, C. ns-μs Time-Resolved Step-Scan FTIR of ba3 Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927. Int. J. Mol. Sci. 2016, 17, 1657.

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