A biosynthetic model of cytochrome c oxidase as an electrocatalyst for oxygen reduction View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-10-12

AUTHORS

Sohini Mukherjee, Arnab Mukherjee, Ambika Bhagi-Damodaran, Manjistha Mukherjee, Yi Lu, Abhishek Dey

ABSTRACT

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. More... »

PAGES

8467

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms9467

DOI

http://dx.doi.org/10.1038/ncomms9467

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1032994332

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26455726


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