Covalent linkage of CYP101 with the electrode enhances the electrocatalytic activity of the enzyme: Vectorial electron transport from the electrode

Mhaske, Sanjay D.; Ray, Moumita; Mazumdar, Shyamalava

doi:10.1016/j.ica.2010.03.054

Cited by 10 publications

(6 citation statements)

References 38 publications

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“…Additionally, pyrene is relatively inert and has already been successfully installed on a broad range of molecular complexes and sensitive biological molecules with desirable catalytic, redox, or sensing properties. [10][11][12][13][14][15][16][17][18][19][20][21][22][23][24] However, this approach of non-covalent attachment had been limited to modifying carbon based electrodes with aromatic character.…”

Section: Introductionmentioning

confidence: 99%

Chemical modification of gold electrodes via non-covalent interactions

Lydon

Germann

Yang

2016

Inorg. Chem. Front.

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Section: Introductionmentioning

confidence: 99%

Chemical modification of gold electrodes via non-covalent interactions

Lydon

Germann

Yang

2016

Inorg. Chem. Front.

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“…48,50−53 The separation between the oxidized and the reduced peak potentials (ΔE p ) at different scan rates (Figure 4 and S5, Supporting Information) is required to determine k app using Laviron's approach. 51,52 3.1.4.1. Apparent Rate Constant of ET (k app ).…”

Section: Results and Analysismentioning

confidence: 99%

“…The rate of heterogeneous ET ( k app ) ,, from the electrode to the iron porphyrin complexes − is determined using Laviron’s method. ,− The separation between the oxidized and the reduced peak potentials (Δ E p ) at different scan rates (Figure and S5, Supporting Information) is required to determine k app using Laviron’s approach. , …”

Section: Results and Analysismentioning

confidence: 99%

“…k app of FeFc 4 and FePf is determined after attaching them to two different SAM surfaces such as Imd-SAM and Thiol-SAM through imidazole and thiolate linkages, respectively. Using Laviron’s method from the cathodic and anodic peak potentials the transfer coefficient (α) can be determined using eqs and , respectively − italicE pc = italicE − ( R T / α n F ) ln [ α / false| italicm false| ] italicE pa = italicE + [ R T / false( 1 − α false) n F ] ln [ false( 1 − α false) / false| italicm false| ] where E pc and E pa are the cathodic and anodic peak potentials, respectively, and E is the formal potential of the redox-active species; here it is the E 1/2 . R , T , n , and F have their usual meaning.…”

Section: Results and Analysismentioning

confidence: 99%

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Effect of Axial Ligand, Spin State, and Hydrogen Bonding on the Inner-Sphere Reorganization Energies of Functional Models of Cytochrome P450

et al. 2014

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Using a combination of self-assembly and synthesis, bioinspired electrodes having dilute iron porphyrin active sites bound to axial thiolate and imidazole axial ligands are created atop self-assembled monolayers (SAMs). Resonance Raman data indicate that a picket fence architecture results in a high-spin (HS) ground state (GS) in these complexes and a hydrogen-bonding triazole architecture results in a low-spin (LS) ground state. The reorganization energies (λ) of these thiolate- and imidazole-bound iron porphyrin sites for both HS and LS states are experimentally determined. The λ of 5C HS imidazole and thiolate-bound iron porphyrin active sites are 10-16 kJ/mol, which are lower than their 6C LS counterparts. Density functional theory (DFT) calculations reproduce these data and indicate that the presence of significant electronic relaxation from the ligand system lowers the geometric relaxation and results in very low λ in these 5C HS active sites. These calculations indicate that loss of one-half a π bond during redox in a LS thiolate bound active site is responsible for its higher λ relative to a σ-donor ligand-like imidazole. Hydrogen bonding to the axial ligand leads to a significant increase in λ irrespective of the spin state of the iron center. The results suggest that while the hydrogen bonding to the thiolate in the 5C HS thiolate bound active site of cytochrome P450 (cyp450) shifts the potential up, resulting in a negative ΔG, it also increases λ resulting in an overall low barrier for the electron transfer process.

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“…To eliminate the need for NADPH we introduced in the 1970s the concept of directly coupling P450s with electrochemical transducers for both sensing and for electrode‐driven substrate conversion . In spite of the large spectrum of P450‐electrode architectures in the literature still the stability and/or catalytic activity are often significantly decreased on the electrode …”

Section: Introductionmentioning

confidence: 99%

Bio‐Electrosynthesis of Vectorially Imprinted Polymer Nanofilms for Cytochrome P450cam

et al. 2019

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A new approach for synthesizing a "vectorially" imprinted polymer (VIP) is presented for the microbial cytochrome P450cam enzyme. A surface attached binding motif of a natural reaction partner of the target protein, putidaredoxin (Pdx), is the anchor to the underlying transducer. The 15 amino acid peptide anchor, which stems from the largest continuous amino acid chain within the binding site of Pdx was modified: (i) internal cysteines were replaced by serines to prevent disulfide bond formation; (ii) 2 ethylene glycol units were attached to the N-terminus as a spacer region; and (iii) an N-terminal cysteine was added to allow the immobilization on the gold electrode surface. Immobilization on GCE was achieved via an N-(1-pyrenyl)maleimide (NPM) cross-linker. In this way oriented immobilization of P450cam was accomplished by binding it to a peptide-modified gold or glassy carbon electrode (GCE) prior to the electrosynthesis of a polymer nanofilm around the immobilized target. This VIP nanofilm enabled reversible oriented docking of P450cam as it is indicated by the catalytic oxygen reduction via direct electron transfer between the enzyme and the underlying electrode. Catalysis of oxygen reduction by P450cam bound to the VIP-modified GCE was used to measure rebinding to the VIP. The "mild" coupling of an oxidoreductase with the electrode may be appropriate for realizing electrodedriven substrate conversion by instable P450 enzymes without the need of NADPH co-factor.

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Covalent linkage of CYP101 with the electrode enhances the electrocatalytic activity of the enzyme: Vectorial electron transport from the electrode

Cited by 10 publications

References 38 publications

Chemical modification of gold electrodes via non-covalent interactions

Chemical modification of gold electrodes via non-covalent interactions

Effect of Axial Ligand, Spin State, and Hydrogen Bonding on the Inner-Sphere Reorganization Energies of Functional Models of Cytochrome P450

Bio‐Electrosynthesis of Vectorially Imprinted Polymer Nanofilms for Cytochrome P450cam

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