Hematin and CuII control generations of hydroperoxyl and superoxide radicals to activate galactose oxidase for 5-hydroxymethylfurfural conversion

Summary: We present a significant finding that Cu(II) ions can activate hematin (Hem) to generate more HOO⋅ and O2⋅- radicals from the decomposition of H2O2. Galactose oxidase (GO) and hematin have been simultaneously immobilized by coordinating to Cu(II) ions (GO&Hem@Cu(II)). The radicals HOO⋅...

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Bibliographic Details
Main Authors: Yao Chen, Jinxin Zou, Peijun Ji, Wei Feng
Format: Article
Language:English
Published: Elsevier 2023-12-01
Series:iScience
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2589004223025294
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Summary:Summary: We present a significant finding that Cu(II) ions can activate hematin (Hem) to generate more HOO⋅ and O2⋅- radicals from the decomposition of H2O2. Galactose oxidase (GO) and hematin have been simultaneously immobilized by coordinating to Cu(II) ions (GO&Hem@Cu(II)). The radicals HOO⋅ and O2⋅- and dioxygen O2 can be in situ generated from the byproduct H2O2 by the Cu(II)-activated hematin. Ample experimental evidence supports the discovery that the immobilized GO is reactivated by the in situ generated HOO⋅ and O2⋅-. For the conversion of 100 mM 5-hydroxymethylfurfural (HMF) in water, GO&Hem@Cu(II) (0.8 mg/mL GO encapsulated) has achieved a 99.5% conversion within 180 min. In contrast, 0.8 mg/mL free GO M3-5 variant (ACS Catalysis 2018, 8, 4025) has achieved an HMF conversion of 17.3%. For the conversion of HMF (1,000 mM) by GO&Hem@Cu(II) (4 mg/mL GO encapsulated), the HMF conversion is 98.8% after 8 h reaction.
ISSN:2589-0042