scholarly journals Ergodicity Breaking in Thermal Biological Electron Transfer? Cytochrome C Revisited II

2020 ◽  
Vol 124 (16) ◽  
pp. 3336-3342
Author(s):  
Zdenek Futera ◽  
Xiuyun Jiang ◽  
Jochen Blumberger
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Ergodicity Breaking ◽  
Biological Electron Transfer

scholarly journals How to Turn an Electron Transfer Protein into a Redox Enzyme for Biosensing

Molecules ◽  
2021 ◽  
Vol 26 (16) ◽  
pp. 4950
Author(s):  
Antonio Ranieri ◽  
Marco Borsari ◽  
Stefano Casalini ◽  
Giulia Di Rocco ◽  
Marco Sola ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Physiological Role ◽  
Self Assembled Monolayers ◽  
Redox Enzyme ◽  
Transfer Protein ◽  
Electron Transfer Protein ◽  
Transport Chain ◽  
Assembled Monolayers ◽  
Biological Electron Transfer

Cytochrome c is a small globular protein whose main physiological role is to shuttle electrons within the mitochondrial electron transport chain. This protein has been widely investigated, especially as a paradigmatic system for understanding the fundamental aspects of biological electron transfer and protein folding. Nevertheless, cytochrome c can also be endowed with a non-native catalytic activity and be immobilized on an electrode surface for the development of third generation biosensors. Here, an overview is offered of the most significant examples of such a functional transformation, carried out by either point mutation(s) or controlled unfolding. The latter can be induced chemically or upon protein immobilization on hydrophobic self-assembled monolayers. We critically discuss the potential held by these systems as core constituents of amperometric biosensors, along with the issues that need to be addressed to optimize their applicability and response.

Sign in / Sign up

Export Citation Format

Share Document