ns-μs Time-Resolved Step-Scan FTIR of ba₃ Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927.
Time-resolved step-scan FTIR spectroscopy has been employed to probe the dynamics of theba₃ oxidoreductase fromThermus thermophilusin 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 hemea₃. 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 hemea₃ is described.
Department of Environmental Science and Technology, Cyprus University of Technology, P.O. Box 50329, 3603 Lemesos, Cyprus. ag.nicolaides@edu.cut.ac.cy.
Antonis
A
Nicolaides
Chemical and Environmental Science Department and Materials & Surface Science Institute, University of Limerick, V94 T9PX Limerick, Ireland. tewfik.soulimane@ul.ie.
Tewfik
T
Soulimane
Department of Environmental Science and Technology, Cyprus University of Technology, P.O. Box 50329, 3603 Lemesos, Cyprus. c.varotsis@cut.ac.cy.
Constantinos
C
Varotsis
cytochrome ba3; heme-copper oxidoreductases; ns time-resolved step-scan FTIR
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