原创力文档site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in cahyda [fefe]-hydrogenase网站饱和突变为半胱氨酸298演示了一个核心作用催化基团的质子给予体cahyda(象皮病)氢化酶.pdfVIP
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site saturation mutagenesis demonstrates a central role for cysteine 298 as proton donor to the catalytic site in cahyda [fefe]-hydrogenase网站饱和突变为半胱氨酸298演示了一个核心作用催化基团的质子给予体cahyda(象皮病)氢化酶
Site Saturation Mutagenesis Demonstrates a Central Role
for Cysteine 298 as Proton Donor to the Catalytic Site in
CaHydA [FeFe]-Hydrogenase
1 1 1 2 1
Simone Morra , Alberto Giraudo , Giovanna Di Nardo , Paul W. King , Gianfranco Gilardi ,
Francesca Valetti1*
1 Department of Life Sciences and Systems Biology, University of Torino, Torino, Italy, 2 Biosciences Center, National Renewable Energy Laboratory, Golden, Colorado,
United States of America
Abstract
[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 the H-cluster and it is important for hydrogenase activity. Here,
the function of C298 in catalysis was investigated in detail by means of site saturation mutagenesis, simultaneously studying
the effect of C298 replacement with all other 19 amino acids and selecting for mutants with high retained activity. We
demonstrated that efficient enzymatic turnover was maintained only when C298 was replaced by aspartic acid, despite the
structural diversity between the two residues. Purified CaHydA C298D does not show any significant structural difference in
terms of secondary structure and iron incorporation, demonstrating that the mutation does not affect the overall protein
fold. C298D retains the hydrogen evolution activity with a decrease of kcat only by 2-fold at pH 8.0 and it caused a shift of
the optimum pH from 8.0 to 7.0. Moreover, the oxygen inactivation rate was not affected demonstrating that the mutation
does not influence O2 diffusion to the active site o
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