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• W2331700810 endingPage "9907" @default.
• W2331700810 startingPage "9897" @default.
• W2331700810 abstract "Bioinspired electrodes have been constructed by physiabsorption of two air stable iron porphyrin complexes, one bearing an imidazole coordination and the other bearing a thiolate coordination. To control the electron transfer (ET) rate to these O2 reducing electrocatalysts, the complexes were immobilized on edge plane graphite electrode and alkyl thiol self-assembled monolayer (SAM) modified Au electrodes with varying chain lengths of the thiols. Catalyst immobilized SAM modified surfaces were characterized using surface enhanced resonance Raman spectroscopy (SERRS), and their electrocatalytic O2 reduction properties were investigated using rotating ring disc electrochemistry (RRDE). While the imidazole bound complex showed increase in partially reduced oxygen species (PROS) on decreasing ET rate, the thiolate bound complex showed the opposite trend, that is, the value of PROS reduced on decreasing the ET rate. SERRS coupled to rotating disc electrochemistry (SERRS-RDE) technique helps gain insight into the O2 reduction mechanism. The results obtained indicate that while the imidazole bound iron porphyrin complex reduces O2 through an inner sphere mechanism using a high-spin (HS) FeII species, the thiolate ligated complex shows an inner sphere as well as outer sphere mechanism using a HS FeII and low-spin (LS) FeII species, respectively. The PROS formation by a HS FeII species of this thiolate bound complex increases with decreasing ET rates while that of a LS FeII species decreases with decreasing ET rates." @default.
• W2331700810 created "2016-06-24" @default.
• W2331700810 creator A5012663625 @default.
• W2331700810 creator A5013392233 @default.
• W2331700810 creator A5027779975 @default.
• W2331700810 creator A5074886355 @default.
• W2331700810 creator A5081129843 @default.
• W2331700810 date "2013-08-20" @default.
• W2331700810 modified "2023-10-07" @default.
• W2331700810 title "Electrocatalytic O₂ Reduction Reaction by Synthetic Analogues of Cytochrome P450 and Myoglobin: In-Situ Resonance Raman and Dynamic Electrochemistry Investigations" @default.
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