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Title: Dioxygen Activation and O–O Bond Formation Reactions by Manganese Corroles

Activation of dioxygen (O 2) in enzymatic and biomimetic reactions has been intensively investigated over the past several decades. More recently, O–O bond formation, which is the reverse of the O 2-activation reaction, has been the focus of current research. Herein, we report the O 2-activation and O–O bond formation reactions by manganese corrole complexes. In the O 2-activation reaction, Mn(V)-oxo and Mn(IV)-peroxo intermediates were formed when Mn(III) corroles were exposed to O 2 in the presence of base (e.g., OH ) and hydrogen atom (H atom) donor (e.g., THF or cyclic olefins); the O 2-activation reaction did not occur in the absence of base and H atom donor. Moreover, formation of the Mn(V)-oxo and Mn(IV)-peroxo species was dependent on the amounts of base present in the reaction solution. The role of the base was proposed to lower the oxidation potential of the Mn(III) corroles, thereby facilitating the binding of O 2 and forming a Mn(IV)-superoxo species. The putative Mn(IV)-superoxo species was then converted to the corresponding Mn(IV)-hydroperoxo species by abstracting a H atom from H atom donor, followed by the O–O bond cleavage of the putative Mn(IV)-hydroperoxo species to form a Mn(V)-oxo species. We have also shown that additionmore » of hydroxide ion to the Mn(V)-oxo species afforded the Mn(IV)-peroxo species via O–O bond formation and the resulting Mn(IV)-peroxo species reverted to the Mn(V)-oxo species upon addition of proton, indicating that the O–O bond formation and cleavage reactions between the Mn(V)-oxo and Mn(IV)-peroxo complexes are reversible. The present paper reports the first example of using the same manganese complex in both O 2-activation and O–O bond formation reactions.« less
 [1] ; ORCiD logo [1] ;  [1] ;  [1] ;  [2] ;  [3] ; ORCiD logo [3] ;  [4] ;  [5] ; ORCiD logo [1] ; ORCiD logo [6]
  1. Ewha Womans Univ., Seoul (Korea, Republic of). Dept. of Chemistry and Nano Science
  2. Univ. of Hyogo (Japan). Picobiology Inst. Graduate School of Life Science
  3. South China Univ. of Technology, Guangzhou (China)
  4. Ewha Womans Univ., Seoul (Korea, Republic of). Dept. of Chemistry and Nano Science; Goa Univ. (India). Dept. of Chemistry
  5. SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource
  6. Ewha Womans Univ., Seoul (Korea, Republic of). Dept. of Chemistry and Nano Science; Chinese Academy of Sciences (CAS), Lanzhou (China). State Key Lab. for Oxo Synthesis and Selective Oxidation. Lanzhou Inst. of Chemical Physics
Publication Date:
Grant/Contract Number:
AC02-76SF00515; P41GM103393; NRF-2012R1A3A2048842; NRF-2010-00353; 2017R1D1A1B03029982; 2017R1D1A1B03032615; 16H02268; 21371059; 21671068
Accepted Manuscript
Journal Name:
Journal of the American Chemical Society
Additional Journal Information:
Journal Volume: 139; Journal Issue: 44; Journal ID: ISSN 0002-7863
American Chemical Society (ACS)
Research Org:
SLAC National Accelerator Lab., Menlo Park, CA (United States); Ewha Womans Univ., Seoul (Korea, Republic of); Univ. of Hyogo (Japan); South China Univ. of Technology, Guangzhou (China)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23); National Inst. of Health (NIH) (United States); National Research Foundation of Korea (NRF); Basic Science Research Program (Korea, Republic of); Ministry of Education, Culture, Sports, Science and Technology (MEXT) (Japan); National Natural Science Foundation of China (NNSFC)
Country of Publication:
United States
OSTI Identifier: