TY - JOUR
T1 - A biosynthetic model of cytochrome c oxidase as an electrocatalyst for oxygen reduction
AU - Mukherjee, Sohini
AU - Mukherjee, Arnab
AU - Bhagi-Damodaran, Ambika
AU - Mukherjee, Manjistha
AU - Lu, Yi
AU - Dey, Abhishek
N1 - Funding Information:
This research is sponsored by Department of Science and Technology, India and US National Institute of Health (GM062211).
Publisher Copyright:
© 2015 Macmillan Publishers Limited. All rights reserved.
PY - 2015/10/12
Y1 - 2015/10/12
N2 - Creating an artificial functional mimic of the mitochondrial enzyme cytochrome c oxidase (CcO) has been a long-term goal of the scientific community as such a mimic will not only add to our fundamental understanding of how CcO works but may also pave the way for efficient electrocatalysts for oxygen reduction in hydrogen/oxygen fuel cells. Here we develop an electrocatalyst for reducing oxygen to water under ambient conditions. We use site-directed mutants of myoglobin, where both the distal Cu and the redox-active tyrosine residue present in CcO are modelled. In situ Raman spectroscopy shows that this catalyst features very fast electron transfer rates, facile oxygen binding and O-O bond lysis. An electron transfer shunt from the electrode circumvents the slow dissociation of a ferric hydroxide species, which slows down native CcO (bovine 500 s-1), allowing electrocatalytic oxygen reduction rates of 5,000 s-1 for these biosynthetic models.
AB - Creating an artificial functional mimic of the mitochondrial enzyme cytochrome c oxidase (CcO) has been a long-term goal of the scientific community as such a mimic will not only add to our fundamental understanding of how CcO works but may also pave the way for efficient electrocatalysts for oxygen reduction in hydrogen/oxygen fuel cells. Here we develop an electrocatalyst for reducing oxygen to water under ambient conditions. We use site-directed mutants of myoglobin, where both the distal Cu and the redox-active tyrosine residue present in CcO are modelled. In situ Raman spectroscopy shows that this catalyst features very fast electron transfer rates, facile oxygen binding and O-O bond lysis. An electron transfer shunt from the electrode circumvents the slow dissociation of a ferric hydroxide species, which slows down native CcO (bovine 500 s-1), allowing electrocatalytic oxygen reduction rates of 5,000 s-1 for these biosynthetic models.
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U2 - 10.1038/ncomms9467
DO - 10.1038/ncomms9467
M3 - Article
C2 - 26455726
AN - SCOPUS:84944145097
SN - 2041-1723
VL - 6
JO - Nature communications
JF - Nature communications
M1 - 8467
ER -
