TY - JOUR
T1 - Electrocatalysis by heme enzymes—applications in biosensing
AU - Zuccarello, Lidia
AU - Barbosa, Catarina
AU - Todorovic, Smilja
AU - Silveira, Célia M.
N1 - Funding Information:
The APC was funded by TIMB3 project, European Union's Horizon 2020 Research and Innovation Program grant agreement No 810856.
Funding Information:
Acknowledgments: We acknowledge the support from Project LISBOA-01-0145-FEDER-007660 (Microbiologia Molecular, Estrutural e Celular) funded by FEDER funds through COMPETE 2020-Programa Operacional Competitividade e Internacionalização (POCI); from FCT—Fundação para a Ciência e a Tecnologia (PTDC/BIA-BFS/31026/2017 and 2020.05017.BD) and from the European Union's Horizon 2020 Research and Innovation Program, through TIMB3 and B-LigZymes projects (grant agreements No 810856 and 824017, respectively). We thank Edilson Galdino for critical reading of the manuscript and helpful discussions.
Funding Information:
Funding: The APC was funded by TIMB3 project, European Union's Horizon 2020 Research and Innovation Program grant agreement No 810856.
Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.
Copyright:
Copyright 2021 Elsevier B.V., All rights reserved.
PY - 2021/2
Y1 - 2021/2
N2 - 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.
AB - 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.
KW - Amperometric biosensor
KW - Chemically modified electrodes
KW - Direct electron transfer
KW - Electrocatalytic activity
KW - Heme enzyme
KW - Mediated electron transfer
KW - Peroxidase
UR - http://www.scopus.com/inward/record.url?scp=85100474563&partnerID=8YFLogxK
U2 - 10.3390/catal11020218
DO - 10.3390/catal11020218
M3 - Review article
AN - SCOPUS:85100474563
VL - 11
SP - 1
EP - 44
JO - Catalysts
JF - Catalysts
SN - 2073-4344
IS - 2
M1 - 218
ER -