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Rationally designed naphthyl substituted amine functionalized ionic liquid platform for covalent immobilization and direct electrochemistry of hemoglobin.

ABSTRACT: Herein, we have designed and demonstrated a facile and effective platform for the covalent anchoring of a tetrameric hemoprotein, hemoglobin (Hb). The platform comprises of naphthyl substituted amine functionalized gel type hydrophobic ionic liquid (NpNH₂-IL) through which the heme protein was covalently attached over a glassy carbon electrode (Hb-NpNH₂-IL/GCE). UV-vis and FT-IR spectral results confirmed that the Hb on NpNH₂-IL retains its native structure, even after being covalently immobilized on NpNH₂-IL platform. The direct electron transfer of redox protein could be realized at Hb-NpNH₂-IL/GCE modified electrode and a well resolved redox peak with a formal potential of -0.30?V and peak separation of 65?mV was observed. This is due to the covalent attachment of highly conducting NpNH₂-IL to the Hb, which facilitates rapid shuttling of electrons between the redox site of protein and the electrode. Further, the fabricated biosensor favoured the electrochemical reduction of bromate in neutral pH with linearity ranging from 12 to 228?µM and 0.228 to 4.42?mM with a detection limit and sensitivities of 3?µM, 430.7?µA?mM^-1 cm^-2 and 148.4?µA?mM^-1 cm^-2 respectively. Notably, the fabricated biosensor showed good operational stability under static and dynamic conditions with high selectivity and reproducibility.

SUBMITTER: Theyagarajan K

PROVIDER: S-EPMC6639313 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature

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Rationally designed naphthyl substituted amine functionalized ionic liquid platform for covalent immobilization and direct electrochemistry of hemoglobin.

Theyagarajan K K Saravanakumar Duraisamy D Senthilkumar Sellappan S Thenmozhi Kathavarayan K

Scientific reports 20190718 1

Herein, we have designed and demonstrated a facile and effective platform for the covalent anchoring of a tetrameric hemoprotein, hemoglobin (Hb). The platform comprises of naphthyl substituted amine functionalized gel type hydrophobic ionic liquid (NpNH2-IL) through which the heme protein was covalently attached over a glassy carbon electrode (Hb-NpNH2-IL/GCE). UV-vis and FT-IR spectral results confirmed that the Hb on NpNH2-IL retains its native structure, even ...[more]

PMID: 31320717

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Project description:Two questions important to the success in metalloenzyme design are how to attach or anchor metal cofactors inside protein scaffolds, and in what way such positioning affects enzymatic properties. We have previously reported a dual anchoring method to position a nonnative cofactor, MnSalen (1), inside the heme cavity of apo sperm whale myoglobin (Mb) and showed that the dual anchoring can increase both the activity and enantioselectivity over the single anchoring methods, making this artificial enzyme an ideal system to address the above questions. Here we report systematic investigations of the effect of different covalent attachment or anchoring positions on reactivity and selectivity of sulfoxidation by the MnSalen-containing Mb enzymes. We have found that changing the left anchor from Y103C to T39C has an almost identical effect of increasing rate by 1.8-fold and increasing selectivity by +14% for S, whether the right anchor is L72C or S108C. At the same time, regardless of the identity of the left anchor, changing the right anchor from S108C to L72C increases rate by 4-fold and selectivity by +66%. The right anchor site was observed to have a greater influence than the left anchor site on the reactivity and selectivity in sulfoxidation of a wide scope of other ortho-, meta- and para- substituted substrates. The 1•Mb(T39C/L72C) showed the highest reactivity (TON up to 2.31 min(-1)) and selectivity (ee% up to 83%) among the different anchoring positions examined. Molecular dynamic simulations indicate that these changes in reactivity and selectivity may be due to the steric effects of the linker arms inside the protein cavity. These results indicate that small differences in the anchor positions can result in significant changes in reactivity and enantioselectivity, probably through steric interactions with substrates when they enter the substrate-binding pocket, and that the effects of right and left anchor positions are independent and additive in nature. The finding that the anchoring arms can influence both the positioning of the cofactor and steric control of substrate entrance will help design better functional metalloenzymes with predicted catalytic activity and selectivity.

Dataset Information

Rationally designed naphthyl substituted amine functionalized ionic liquid platform for covalent immobilization and direct electrochemistry of hemoglobin.

Publications

Rationally designed naphthyl substituted amine functionalized ionic liquid platform for covalent immobilization and direct electrochemistry of hemoglobin.

Similar Datasets

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