Mus-Veteau I, Guerlesquin F
Laboratoire de Chimie Bactérienne, Centre National de la Recherche Scientifique (CNRS), Marseille, France.
Biochem Biophys Res Commun. 1994 May 30;201(1):128-34. doi: 10.1006/bbrc.1994.1678.
In spite of their structural and amino acid sequence differences, Fe-only and Ni-containing hydrogenases achieved the same catalytic reactions. A chemical modification of histidine residues using a highly specific reagent (pentaammineruthenium II) has been carried out on Desulfovibrio vulgaris Hildenborough Fe-hydrogenase and Desulfovibrio desulfuricans Norway Ni-Fe-Se-hydrogenase. The preliminary results obtained suggest the existence of a general mechanism involving histidine residues in the two groups of hydrogenases. These residues may be part of the histidine-containing motive shown to be present in both Fe- and Ni-Fe-hydrogenase sequences by Hydrophobic Cluster Analysis. This analysis also allows us to suggest a functional role for the small subunit of Desulfovibrio vulgaris Hildenborough Fe-hydrogenase.
尽管仅含铁的氢化酶和含镍的氢化酶在结构和氨基酸序列上存在差异，但它们实现了相同的催化反应。已使用一种高度特异性试剂（五氨合钌II）对希登伯勒脱硫弧菌铁氢化酶和挪威脱硫脱硫弧菌镍铁硒氢化酶的组氨酸残基进行了化学修饰。所获得的初步结果表明，这两类氢化酶存在一种涉及组氨酸残基的通用机制。这些残基可能是通过疏水簇分析显示在铁氢化酶和镍铁氢化酶序列中均存在的含组氨酸基序的一部分。该分析还使我们能够推测希登伯勒脱硫弧菌铁氢化酶小亚基的功能作用。
