Electrocatalysis by heme enzymes—applications in biosensing

Lidia Zuccarello, Catarina Barbosa, Smilja Todorovic, Célia M. Silveira

Research output: Contribution to journalReview articlepeer-review

3 Citations (Scopus)
1 Downloads (Pure)

Abstract

Heme proteins take part in a number of fundamental biological processes, including oxygen transport and storage, electron transfer, catalysis and signal transduction. The redox chemistry of the heme iron and the biochemical diversity of heme proteins have led to the development of a plethora of biotechnological applications. This work focuses on biosensing devices based on heme proteins, in which they are electronically coupled to an electrode and their activity is determined through the measurement of catalytic currents in the presence of substrate, i.e., the target analyte of the biosensor. After an overview of the main concepts of amperometric biosensors, we address transduction schemes, protein immobilization strategies, and the performance of devices that explore reactions of heme biocatalysts, including peroxidase, cytochrome P450, catalase, nitrite reductase, cytochrome c oxidase, cytochrome c and derived microperoxidases, hemoglobin, and myoglobin. We further discuss how structural information about immobilized heme proteins can lead to rational design of biosensing devices, ensuring insights into their efficiency and long-term stability.

Original languageEnglish
Article number218
Pages (from-to)1-44
Number of pages44
JournalCatalysts
Volume11
Issue number2
DOIs
Publication statusPublished - Feb 2021

Keywords

  • Amperometric biosensor
  • Chemically modified electrodes
  • Direct electron transfer
  • Electrocatalytic activity
  • Heme enzyme
  • Mediated electron transfer
  • Peroxidase

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