The H93G myoglobin cavity mutant as a versatile scaffold for modeling heme iron coordination structures in protein active sites and their characterization with magnetic circular dichroism spectroscopyJing Du, John H. Dawson, Masanori Sono|Coordination Chemistry Reviews|2011Cited by 52
Functional Switching of <i>Amphitrite ornata</i> Dehaloperoxidase from O<sub>2</sub>-Binding Globin to Peroxidase Enzyme Facilitated by Halophenol Substrate and H<sub>2</sub>O<sub>2</sub>Jing Du, John H. Dawson, Masanori Sono|Biochemistry|2010Cited by 42
Influence of heme environment structure on dioxygen affinity for the dual function Amphitrite ornata hemoglobin/dehaloperoxidase. Insights into the evolutional structure–function adaptationsShengfang Sun, John H. Dawson, Chunxue Wang et al.|Archives of Biochemistry and Biophysics|2014Cited by 23
Evidence of the Direct Involvement of the Substrate TCP Radical in Functional Switching from Oxyferrous O<sub>2</sub> Carrier to Ferric Peroxidase in the Dual-Function Hemoglobin/Dehaloperoxidase from <i>Amphitrite ornata</i>Shengfang Sun, John H. Dawson, Masanori Sono et al.|Biochemistry|2014Cited by 14
The proximal and distal pockets of the H93G myoglobin cavity mutant bind identical ligands with different affinities: Quantitative analysis of imidazole and pyridine bindingJing Du, John H. Dawson, Masanori Sono|Spectroscopy An International Journal|2008Cited by 9