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Commissariat à lEnergie Atomique, Institut de Biologie et de Technologies de Saclay, Service de Bioénergétique, Biologie Structurale et Mécanismes CNRS UMR-8221, Gif-sur-Yvette Cedex 91191, France

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Leiden Institute of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Niels Bohrweg 2, PO Box 9504, RA Leiden 2300, The Netherlands





*

Author to whom correspondence should be addressed.



Abstract Nature utilizes oxido-reductases to cater to the energy demands of most biochemical processes in respiratory species. Oxido-reductases are capable of meeting this challenge by utilizing redox active sites, often containing transition metal ions, which facilitate movement and relocation of electrons-protons to create a potential gradient that is used to energize redox reactions. There has been a consistent struggle by researchers to estimate the electron transfer rate constants in physiologically relevant processes. This review provides a brief background on the measurements of electron transfer rates in biological molecules, in particular Cu-containing enzymes, and highlights the recent advances in monitoring these electron transfer events at the single molecule level or better to say, at the individual event level. View Full-Text

Keywords: electron transfer; random sequential; single molecule; enzyme; FRET; redox; nitrite reductase; small laccase; copper protein; ABEL trap electron transfer; random sequential; single molecule; enzyme; FRET; redox; nitrite reductase; small laccase; copper protein; ABEL trap





Autor: Leandro C. Tabares 1, Ankur Gupta 2, Thijs J. Aartsma 2 and Gerard W. Canters 2,*

Fuente: http://mdpi.com/



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