Site Saturation Mutagenesis Demonstrates a Central Role for Cysteine 298 as Proton Donor to the Catalytic Site in CaHydA [FeFe]-Hydrogenase

[FeFe]-hydrogenases reversibly catalyse molecular hydrogen evolution by reduction of two protons. Proton supply to the catalytic site (H-cluster) is essential for enzymatic activity. Cysteine 298 is a highly conserved residue in all [FeFe]-hydrogenases; moreover C298 is structurally very close to th...

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Autores principales: Morra, Simone, Giraudo, Alberto, Di Nardo, Giovanna, King, Paul W., Gilardi, Gianfranco, Valetti, Francesca
Formato: Artigo
Lenguaje:Inglês
Publicado: Public Library of Science 2012
Materias:
Research Article
Acceso en línea:https://ncbi.nlm.nih.gov/pmc/articles/PMC3485046/
https://ncbi.nlm.nih.gov/pubmed/23133586
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0048400
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