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.

Self-assembled monolayers of optically active Co(iii) complexes: a new promoter electrode recognizing the electron transfer site in cytochrome c

2005 ◽  
pp. 471 ◽  
Author(s):  
Isao Takahashi ◽  
Tomohiko Inomata ◽  
Yasuhiro Funahashi ◽  
Tomohiro Ozawa ◽  
Koichiro Jitsukawa ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Optically Active ◽  
Self Assembled Monolayers ◽  
Assembled Monolayers ◽  
Self Assembled

scholarly journals The crystal structure of the pentahaem c-type cytochrome NrfB and characterization of its solution-state interaction with the pentahaem nitrite reductase NrfA

2007 ◽  
Vol 406 (1) ◽  
pp. 19-30 ◽  
Author(s):  
Thomas A. Clarke ◽  
Jeffrey A. Cole ◽  
David J. Richardson ◽  
Andrew M. Hemmings
Keyword(s):  
Crystal Structure ◽  
Nitric Oxide ◽  
Electron Transfer ◽  
Physiological Role ◽  
Enteric Bacteria ◽  
Nitrite Reduction ◽  
Protein Protein Interaction ◽  
Transfer Protein ◽  
Electron Transfer Protein ◽  
Nitric Oxide Reduction

NrfB is a small pentahaem electron-transfer protein widely involved in the respiratory reduction of nitrite or nitric oxide to ammonia, processes that provide energy for anaerobic metabolism in many enteric bacteria and also serve to detoxify these reactive nitrogen species. The X-ray crystal structure of Escherichia coli NrfB is presented at 1.74 Å (1 Å=0.1 nm) resolution. The architecture of the protein is that of a 40 Å ‘nanowire’ in which the five haems are positioned within 6 Å of each other along a polypeptide scaffold. During nitrite reduction, the physiological role of NrfB is to mediate electron transfer to another pentahaem protein, NrfA, the enzyme that catalyses periplasmic nitrite or nitric oxide reduction. Protein–protein interaction studies suggest NrfA and NrfB can form a 20-haem NrfA2–NrfB2 heterotetrameric complex.

Evaluation of the Tunneling Constant for Long Range Electron Transfer in Azobenzene Self-Assembled Monolayers on Gold

Langmuir ◽  
1997 ◽  
Vol 13 (21) ◽  
pp. 5774-5778 ◽  
Author(s):  
H. Z. Yu ◽  
H. B. Shao ◽  
Y. Luo ◽  
H. L. Zhang ◽  
Z. F. Liu
Keyword(s):  
Electron Transfer ◽  
Long Range ◽  
Self Assembled Monolayers ◽  
Assembled Monolayers ◽  
Self Assembled
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