Manganese protoporphyrin IX reconstituted myoglobin capable of epoxidation of the C=C bond with Oxone (R)

Replacement of the native heme cofactor by manganese protoporphyrin IX (MnPPIX) to reconstitute manganese myoglobin (Mn(III)Mb) is an important approach to investigate the reactivity of the Mn center inside protein scaffolds. However, unlike the Mn porphyrin synthetic model compounds, MnPPIX reconst...

Full description

Bibliographic Details
Published in:Inorganic Chemistry Frontiers
Main Authors: Cai, Yuan-Bo, Yao, Si-Yu, Hu, Mo, Liu, Xiaoyun, Zhang, Jun-Long
Other Authors: Zhang, JL (reprint author), Peking Univ, Coll Chem & Mol Engn, State Key Lab Rare Earth Mat Chem & Applicat, Beijing Natl Lab Mol Sci, Beijing 100871, Peoples R China.; Liu, XY (reprint author), Peking Univ, Inst Analyt Chem, Beijing 100871, Peoples R China.; Liu, XY (reprint author), Peking Univ, Synthet & Funct Biomol Ctr, Coll Chem & Mol Engn, Beijing 100871, Peoples R China., Peking Univ, Coll Chem & Mol Engn, State Key Lab Rare Earth Mat Chem & Applicat, Beijing Natl Lab Mol Sci, Beijing 100871, Peoples R China., Peking Univ, Inst Analyt Chem, Beijing 100871, Peoples R China., Peking Univ, Synthet & Funct Biomol Ctr, Coll Chem & Mol Engn, Beijing 100871, Peoples R China., Liu, XY (reprint author), Peking Univ, Inst Analyt Chem, Beijing 100871, Peoples R China., Liu, XY (reprint author), Peking Univ, Synthet & Funct Biomol Ctr, Coll Chem & Mol Engn, Beijing 100871, Peoples R China.
Format: Journal/Newspaper
Language:English
Published: INORGANIC CHEMISTRY FRONTIERS 2016
Subjects:
CYTOCHROME-C PEROXIDASE
SPERM-WHALE MYOGLOBIN
OXYGEN-ATOM TRANSFER
SUBSTITUTED HORSERADISH-PEROXIDASE
HYDROGEN-PEROXIDE
OXOMANGANESE(V) PORPHYRIN
CATALYTIC-PROPERTIES
DISTAL HISTIDINES
AQUEOUS-SOLUTION
COMPOUND-I
Sperm whale
Online Access:https://hdl.handle.net/20.500.11897/459168
https://doi.org/10.1039/c6qi00120c
Description
Summary:Replacement of the native heme cofactor by manganese protoporphyrin IX (MnPPIX) to reconstitute manganese myoglobin (Mn(III)Mb) is an important approach to investigate the reactivity of the Mn center inside protein scaffolds. However, unlike the Mn porphyrin synthetic model compounds, MnPPIX reconstituted myoglobins (Mn(III)Mb) have no reactivity in the epoxidation of styrene using H2O2, which was attributed to the low reactivity of the Mn-IV=O intermediate after homocleavage of the O-O bond in manganese peroxide. To address this issue, we herein chose Oxone (R) (2KHSO(5)center dot KHSO4 center dot K2SO4), a well-known oxidant undergoing O-O bond heterocleavage. After screening 7 mutants and wild-type Mn(III)Mb, we found that the L29H/F43H mutant could generate a new species ([Mn-IV=O]+(center dot)), tentatively assigned by using UV-vis and EPR spectra, through heterocleavage of the O-O bond. Computational docking showed hydrogen bonds between three distal histidines (H64, L29H and F43H) and anions, which increase the binding affinity to persulfate. With Oxone (R) as the oxidant, Mn(III)Mb (L29H/F43H) showed the highest reactivity toward the epoxidation of styrene, different from that with the H2O2 oxidant. This work demonstrates the first example of MnPPIX reconstituted Mb which could catalyze styrene epoxidation and provides new insights to further explore the reactivity of the Mn center in protein scaffolds. National Scientific Foundation of China [20971007, 21101169, 21271013, 21571007]; National Key Basic Research Support Foundation of China (NKBRSFC) [2010CB912302, 2015CB856300, 2015CB856301] SCI(E) ARTICLE xiaoyun.liu@pku.edu.cn; zhangjunlong@pku.edu.cn 10 1236-1244 3

Similar Items