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<p>TiO<sub>2</sub> with iron–porphyrin complex functionalization is proposed to act as hemoglobin accommodation matrix via multiple mutual interactions between elements of nano-complex and integrated heme protein including the competitive ligation. The spectrometric and electrochemical techniques are used to explore the influences of the mutual interactions on the electron transferring mechanism, electro-catalytic kinetics and the photo-electrocatalytic performance of nano-complex with protein immobilization. The electrochemical reaction occurred on hemoglobin based electrode consists of two concurrent redox processes and it is dominated by cofactors of hemoglobin in coordination with porphyrin derivative. Such redox processes indicate one electro-chemical reaction for heme sites of hemoglobin ligation with porphyrin ring with favorable electron shuttle efficiency (0.54&#xa0;s<sup>−1</sup>) and another one for electro-active sites onto TiO<sub>2</sub> with inferior activity. The redox process of such electrode could be classified into a typical quasi-reversible surface-controlling reaction with four electrons and two protons participation involvement. Such competitive ligation would debase H<sub>2</sub>O<sub>2</sub> transformation with inferior dynamics (0.38&#xa0;s<sup>−1</sup>). The emulous complexation would increase the photo-electrical conversion efficiency remarkably. However, such competitive coordination could not be regarded as the decisive factor in restricting the electro-catalytic performance because the substrate diffusion is supposed to be the rate-determining step (6.7 × 10<sup>–2</sup>&#xa0;s<sup>−1</sup>).</p> Graphical abstract <p> The competitive coordination between porphyrin-like chemical: TCPP and heme site in hemoglobin molecule would produce the intermediate species with the unique spectroscopic and electrochemical features.</p>

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The direct electron transferring and evaluation on its electro-chemical sensing performance on hydrogen peroxide for the electrode on the basis of iron–porphyrin complex-functionalized nano-titanium dioxide with hemoglobin anchoring

  • 期刊论文

  • 发表日期：

    2025年6月27日

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  • Min Zhang,
  • Bao Chen Han,
  • Han Yan Dai,
  • Han Zeng

摘要

TiO2 with iron–porphyrin complex functionalization is proposed to act as hemoglobin accommodation matrix via multiple mutual interactions between elements of nano-complex and integrated heme protein including the competitive ligation. The spectrometric and electrochemical techniques are used to explore the influences of the mutual interactions on the electron transferring mechanism, electro-catalytic kinetics and the photo-electrocatalytic performance of nano-complex with protein immobilization. The electrochemical reaction occurred on hemoglobin based electrode consists of two concurrent redox processes and it is dominated by cofactors of hemoglobin in coordination with porphyrin derivative. Such redox processes indicate one electro-chemical reaction for heme sites of hemoglobin ligation with porphyrin ring with favorable electron shuttle efficiency (0.54 s−1) and another one for electro-active sites onto TiO2 with inferior activity. The redox process of such electrode could be classified into a typical quasi-reversible surface-controlling reaction with four electrons and two protons participation involvement. Such competitive ligation would debase H2O2 transformation with inferior dynamics (0.38 s−1). The emulous complexation would increase the photo-electrical conversion efficiency remarkably. However, such competitive coordination could not be regarded as the decisive factor in restricting the electro-catalytic performance because the substrate diffusion is supposed to be the rate-determining step (6.7 × 10–2 s−1).

Graphical abstract

The competitive coordination between porphyrin-like chemical: TCPP and heme site in hemoglobin molecule would produce the intermediate species with the unique spectroscopic and electrochemical features.