Various functions of selenols and thiols in anaerobic Gram-positive, amino acids-utilizing bacteria

被引:34
作者
Andreesen, JR [1 ]
Wagner, M [1 ]
Sonntag, D [1 ]
Kohlstock, M [1 ]
Harms, C [1 ]
Gursinsky, T [1 ]
Jäger, J [1 ]
Parther, T [1 ]
Kabisch, U [1 ]
Gräntzdörffer, A [1 ]
Pich, A [1 ]
Söhling, B [1 ]
机构
[1] Univ Halle Wittenberg, Inst Mikrobiol, D-06120 Halle, Germany
关键词
selenocysteine; Gram-positive bacteria; anaerobic reductase systems; peroxiredoxins; proprotein processing;
D O I
10.1002/biof.5520100226
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Electron transfer reactions for the reduction of glycine in Eubacterium acidaminophilum involve many selenocysteine (U)- and thiol-containing proteins, as shown by biochemical and molecular analysis. These include an unusual thioredoxin system (-CXXC-), protein A (-CXXU-) and the substrate-specific protein B of glycine reductase (-UXXCXXC-). Most probably a selenoether is formed at protein B by splitting the C-N-bond after binding of the substrate. The carboxymethyl group is then transferred to the selenocysteine of protein A containing a conserved motif. The latter protein acts as a carbon and electron donor by giving rise to a protein C-bound acetyl-thioester and a mixed selenide-sulfide bond at protein A that will be reduced by the thioredoxin system. The dithiothreitol-dependent D-proline reductase of Clostridium sticklandii exhibits many similarities to protein B of glycine reductase including the motif containing selenocysteine. In both cases proprotein processing at a cysteine residue gives rise to a blocked N-terminus, most probably a pyruvoyl group. Formate dehydrogenase and some other proteins from E. acidaminophilum contain selenocysteine, e.g., a 22 kDa protein showing an extensive homology to peroxiredoxins involved in the detoxification of peroxides.
引用
收藏
页码:263 / 270
页数:8
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