The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation
The development of artificial metalloenzymes is an expanding field, involving various protein scaffolds and incorporating a wide range of transition-metal catalysts. Due to its pH-dependent disassembling properties, apoferritin has been used extensively for various purposes. However, very few studie...
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| Format: | Thesis (University of Nottingham only) |
| Language: | English |
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2018
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| Online Access: | https://eprints.nottingham.ac.uk/53544/ |
| _version_ | 1848798954976706560 |
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| author | Hoteit, Camille |
| author_facet | Hoteit, Camille |
| author_sort | Hoteit, Camille |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | The development of artificial metalloenzymes is an expanding field, involving various protein scaffolds and incorporating a wide range of transition-metal catalysts. Due to its pH-dependent disassembling properties, apoferritin has been used extensively for various purposes. However, very few studies reported its use as a scaffold for the design of artificial metalloenzymes.
This study investigated the development of an apoferritin-based artificial metalloenzyme, based on covalent conjugation with a manganese-salen complex, applied to the catalysis of sulphide oxidation.
A mouse recombinant heavy-chain apoferritin mutant, containing a unique and reactive cysteine, in position 68, pointing towards its hollow core, was expressed and purified. A manganese-salen bearing a maleimide linker was synthesised and covalently linked to apoferritin’s cysteine 68, via a Michael addition reaction.
The catalytic activity towards the enantioselective oxidation of thioanisole was assessed in both organic and aqueous media and has resulted in pH-dependent activity and enantioselectivity, with up to 69 % conversion and 17 % ee, due to the reassembling of the conjugated apoferritin nanocapsule.
However, background reactions exhibited high yields in certain conditions and the stability of the apoferritin-based artificial metalloenzyme was extremely relative at pH ranges where native apoferritin was supposed to be stable. Therefore, further research is recommended to improve three key features of this catalyst: stability, enantioselectivity and reactivity. |
| first_indexed | 2025-11-14T20:27:59Z |
| format | Thesis (University of Nottingham only) |
| id | nottingham-53544 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T20:27:59Z |
| publishDate | 2018 |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-535442025-02-28T14:13:28Z https://eprints.nottingham.ac.uk/53544/ The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation Hoteit, Camille The development of artificial metalloenzymes is an expanding field, involving various protein scaffolds and incorporating a wide range of transition-metal catalysts. Due to its pH-dependent disassembling properties, apoferritin has been used extensively for various purposes. However, very few studies reported its use as a scaffold for the design of artificial metalloenzymes. This study investigated the development of an apoferritin-based artificial metalloenzyme, based on covalent conjugation with a manganese-salen complex, applied to the catalysis of sulphide oxidation. A mouse recombinant heavy-chain apoferritin mutant, containing a unique and reactive cysteine, in position 68, pointing towards its hollow core, was expressed and purified. A manganese-salen bearing a maleimide linker was synthesised and covalently linked to apoferritin’s cysteine 68, via a Michael addition reaction. The catalytic activity towards the enantioselective oxidation of thioanisole was assessed in both organic and aqueous media and has resulted in pH-dependent activity and enantioselectivity, with up to 69 % conversion and 17 % ee, due to the reassembling of the conjugated apoferritin nanocapsule. However, background reactions exhibited high yields in certain conditions and the stability of the apoferritin-based artificial metalloenzyme was extremely relative at pH ranges where native apoferritin was supposed to be stable. Therefore, further research is recommended to improve three key features of this catalyst: stability, enantioselectivity and reactivity. 2018-12-12 Thesis (University of Nottingham only) NonPeerReviewed application/pdf en arr https://eprints.nottingham.ac.uk/53544/1/Thesis_Camille%20Hoteit_4240622_Corrected.pdf Hoteit, Camille (2018) The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation. MPhil thesis, University of Nottingham. Artificial metalloenzyme; Biocatalysis; Apoferritin; Salen; Sulfoxidation |
| spellingShingle | Artificial metalloenzyme; Biocatalysis; Apoferritin; Salen; Sulfoxidation Hoteit, Camille The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation |
| title | The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation |
| title_full | The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation |
| title_fullStr | The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation |
| title_full_unstemmed | The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation |
| title_short | The development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation |
| title_sort | development of an apoferritin-based artificial metalloenzyme for catalysis of sulfide oxidation |
| topic | Artificial metalloenzyme; Biocatalysis; Apoferritin; Salen; Sulfoxidation |
| url | https://eprints.nottingham.ac.uk/53544/ |