Observation of Ligand Transfer in ba3 Oxidase from Thermus thermophilus: Simultaneous FTIR Detection of Photolabile Heme a32+–CN and Transient CuB2+–CN Complexes
Author:
Affiliation:
1. Department of Chemistry, University of Cyprus, P.O. Box 20537, 1678 Nicosia, Cyprus
2. Chemical and Environmental Sciences Department and Materials & Surface Science Institute, University of Limerick, Limerick, Ireland
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/jp305096y
Reference37 articles.
1. Than, M. E.; Soulimane, T.Handbook of Metalloproteins;Wiley:New York, 2001; pp363–378.
2. Structure and mechanism of the aberrant ba3-cytochrome c oxidase from Thermus thermophilus
3. The heme-copper oxidases of Thermus thermophilus catalyze the reduction of nitric oxide: Evolutionary implications
4. Magnetic circular dichroism study of cytochrome ba3 from Thermus thermophilus: spectral contributions from cytochromes b and a3 and nanosecond spectroscopy of carbon monoxide photodissociation intermediates
5. Kinetic Properties of ba3 Oxidase from Thermus thermophilus: Effect of Temperature
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1. Reversible temperature-dependent high- to low-spin transition in the heme Fe–Cu binuclear center of cytochrome ba3 oxidase;RSC Advances;2019
2. ns-μs Time-Resolved Step-Scan FTIR of ba3 Oxidoreductase from Thermus thermophilus: Protonic Connectivity of w941-w946-w927;International Journal of Molecular Sciences;2016-09-29
3. 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;2016-09
4. Detection of functional hydrogen-bonded water molecules with protonated/deprotonated key carboxyl side chains in the respiratory enzyme ba3-oxidoreductase;Physical Chemistry Chemical Physics;2015
5. The structure of a ferrous heme-nitro species in the binuclear heme a3/CuB center of ba3-cytochrome c oxidase as determined by resonance Raman spectroscopy;Chemical Communications;2015
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