期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 139, 期 35, 页码 12209-12218出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.7b05800
关键词
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资金
- U.S. National Institutes of Health (NIH) [5T32-GM070421, NIH R01GM06211, NIH R01GM074785]
- NIH [5T32-GM8276-24]
- U.S. National Science Foundation (NSF) [NSF CHE-1300912]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-ACO2-76SF00515]
- Department of Energy Office of Biological and Environmental Research
- NIH National Institute of General Medical Sciences (NIHMS)
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1300912] Funding Source: National Science Foundation
The presence of a nonheme metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzymatic activity of reducing O-2 to H2O, but the exact mechanism the nonheme metal ion uses to confer and fine-tune the activity remains to be understood. We herein report that manganese and cobalt can bind to the same nonheme site and confer HCO activity in a heme nonheme biosynthetic model in myoglobin. While the initial rates of 02 reduction by the Mn, Fe, and Co derivatives are similar, the percentages of reactive oxygen species (ROS) formation are 7%, 4%, and 1% and the total turnovers are 5.1 +/- 1.1, 13.4 +/- 0.7, and 82.5 +/- 2.5, respectively. These results correlate with the trends of nonheme-metal-binding dissociation constants (35, 22, and 9 mu M) closely, suggesting that tighter metal binding can prevent ROS release from the active site, lessen damage to the protein, and produce higher total turnover numbers. Detailed spectroscopic, electrochemical, and computational studies found no evidence of redox cycling of manganese or cobalt in the enzymatic reactions and suggest that structural and electronic effects related to the presence of different nonheme metals lead to the observed differences in reactivity. This study of the roles of nonheme metal ions beyond the Cu and Fe found in native enzymes has provided deeper insights into nature's choice of metal ion and reaction mechanism and allows for finer control of the enzymatic activity, which is a basis for the design of efficient catalysts for the oxygen reduction reaction in fuel cells.
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