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Bacterial molybdoenzymes: old enzymes for new purposes
Author(s) -
Silke Leimkühler,
Chantal IobbiNivol
Publication year - 2015
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1093/femsre/fuv043
Subject(s) - molybdenum cofactor , cofactor , bacteria , molybdenum , biochemistry , microbial metabolism , enzyme , biology , anaerobic bacteria , nitrate reductase , assimilation (phonology) , metabolism , archaea , chemistry , genetics , inorganic chemistry , linguistics , philosophy
Molybdoenzymes are widespread in eukaryotic and prokaryotic organisms where they play crucial functions in detoxification reactions in the metabolism of humans and bacteria, in nitrate assimilation in plants and in anaerobic respiration in bacteria. To be fully active, these enzymes require complex molybdenum-containing cofactors, which are inserted into the apoenzymes after folding. For almost all the bacterial molybdoenzymes, molybdenum cofactor insertion requires the involvement of specific chaperones. In this review, an overview on the molybdenum cofactor biosynthetic pathway is given together with the role of specific chaperones dedicated for molybdenum cofactor insertion and maturation. Many bacteria are involved in geochemical cycles on earth and therefore have an environmental impact. The roles of molybdoenzymes in bioremediation and for environmental applications are presented.

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