analyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [nife] hydrogenases大亚基富含组氨酸的分析主题暴露另一个质子转移途径在镍铁氢化酶.pdfVIP

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analyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [nife] hydrogenases大亚基富含组氨酸的分析主题暴露另一个质子转移途径在镍铁氢化酶.pdf

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analyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [nife] hydrogenases大亚基富含组氨酸的分析主题暴露另一个质子转移途径在镍铁氢化酶

Analyses of the Large Subunit Histidine-Rich Motif Expose an Alternative Proton Transfer Pathway in [NiFe] Hydrogenases ´ 1 ´ 2 ´ 3 4 ´ ´ 1,4 Emma Szo˝ ri-Doroghazi , Gergely Maroti , Milan Szo˝ ri , Andrea Nyilasi , Gabor Rakhely *, ´ ´ 1,4 Kornel L. Kovacs ´ 1 Department of Biotechnology, University of Szeged, Szeged, Hungary, 2 BayGen Institute, Bay Zoltan Foundation for Applied Research, Szeged, Hungary, 3 Department ´ of Chemical Informatics, Juhasz Gyula Faculty of Education, University of Szeged, Szeged, Hungary, 4 Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences, Szeged, Hungary Abstract A highly conserved histidine-rich region with unknown function was recognized in the large subunit of [NiFe] hydrogenases. The HxHxxHxxHxH sequence occurs in most membrane-bound hydrogenases, but only two of these histidines are present in the cytoplasmic ones. Site-directed mutagenesis of the His-rich region of the T. roseopersicina membrane-attached Hyn hydrogenase disclosed that the enzyme activity was significantly affected only by the replacement of the His104 residue. Computational analysis of the hydrogen bond network in the large subunits indicated that the second histidine of this motif might be a component of a proton transfer pathway including Arg487, Asp103, His104 and Glu436. Substitutions of the conserved amino acids of the presumed transfer route impaired the activity of the Hyn hydrogenase. Western hybridization was applied to demonstrate tha