Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 137, Issue 36, Pages 11570-11573Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b07119
Keywords
-
Categories
Funding
- U.S. National Institutes of Health [GM06221]
- Major State Basic Research Program of China [2015CB856203]
- National Natural Science Foundation of China [21325211, 91313301, 81302687, 31270859]
- Innovation Fund for Technology Based Firms [14C26211100178]
- Tianjin Municipal Grants [14ZCZDSY00059, 14JCYBJC43400]
- Youth Innovation Promotion Association of the Chinese Academy of Sciences
Ask authors/readers for more resources
Terminal oxidases catalyze four-electron reduction of oxygen to water, and the energy harvested is utilized to drive the synthesis of adenosine triphosphate. While much effort has been made to design a catalyst mimicking the function of terminal oxidases, most biomimetic catalysts have much lower activity than native oxidases. Herein we report a designed oxidase in myoglobin with an O-2 reduction rate (52 s(-1)) comparable to that of a native cytochrome (cyt) cbb(3) oxidase (SO s(-1)) under identical conditions. We achieved this goal by engineering more favorable electrostatic interactions between a functional oxidase model designed in sperm whale myoglobin and its native redox partner, cyt b(5), resulting in a 400-fold electron transfer (ET) rate enhancement. Achieving high activity equivalent to that of native enzymes in a designed metalloenzyme offers deeper insight into the roles of tunable processes such as ET in oxidase activity and enzymatic function and may extend into applications such as more efficient oxygen reduction reaction catalysts for biofuel cells.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available