Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site

[Image: see text] The redox chemistry of the electron entry/exit site in Escherichia coli hydrogenase-1 is shown to play a vital role in tuning biocatalysis. Inspired by nature, we generate a HyaA-R193L variant to disrupt a proposed Arg–His cation−π interaction in the secondary coordination sphere o...

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Detalles Bibliográficos
Autores principales: Adamson, Hope, Robinson, Martin, Wright, John J., Flanagan, Lindsey A., Walton, Julia, Elton, Darrell, Gavaghan, David J., Bond, Alan M., Roessler, Maxie M., Parkin, Alison
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2017
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5562392/
https://www.ncbi.nlm.nih.gov/pubmed/28697596
http://dx.doi.org/10.1021/jacs.7b03611

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5562392/
https://www.ncbi.nlm.nih.gov/pubmed/28697596
http://dx.doi.org/10.1021/jacs.7b03611

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