Oxygen-linked Equilibrium CuB-CO Species in Cytochrome ba3 Oxidase from Thermus thermophilus
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference12 articles.
1. Structure and mechanism of the aberrant ba3-cytochrome c oxidase from Thermus thermophilus
2. Handbook of Metalloproteins;Than,2001
3. The heme-copper oxidases of Thermus thermophilus catalyze the reduction of nitric oxide: Evolutionary implications
4. Kinetic Properties of ba3 Oxidase from Thermus thermophilus: Effect of Temperature
5. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
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1. Discrete Ligand Binding and Electron Transfer Properties of ba3-Cytochrome c Oxidase from Thermus thermophilus: Evolutionary Adaption to Low Oxygen and High Temperature Environments;Accounts of Chemical Research;2019-04-25
2. Reversible temperature-dependent high- to low-spin transition in the heme Fe–Cu binuclear center of cytochrome ba3 oxidase;RSC Advances;2019
3. Role of the Conserved Valine 236 in Access of Ligands to the Active Site of Thermus thermophilus ba3 Cytochrome Oxidase;Biochemistry;2016-12-27
4. 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
5. 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
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