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Molybdenum enzymes, their maturation and molybdenum cofactor biosynthesis in Escherichia coli

  • Molybdenum cofactor (Moco) biosynthesis is an ancient, ubiquitous, and highly conserved pathway leading to the biochemical activation of molybdenum. Moco is the essential component of a group of redox enzymes, which are diverse in terms of their phylogenetic distribution and their architectures, both at the overall level and in their catalytic geometry. A wide variety of transformations are catalyzed by these enzymes at carbon, sulfur and nitrogen atoms, which include the transfer of an oxo group or two electrons to or from the substrate. More than 50 molybdoenzymes were identified in bacteria to date. In molybdoenzymes Mo is coordinated to a dithiolene group on the 6-alkyl side chain of a pterin called molybdopterin (MPT). The biosynthesis of Moco can be divided into four general steps in bacteria: I) formation of the cyclic pyranopterin monophosphate, 2) formation of MPT, 3) insertion of molybdenum into molybdopterin to form Moco, and 4) additional modification of Moco with the attachment of GMP or CMP to the phosphate group of MPT,Molybdenum cofactor (Moco) biosynthesis is an ancient, ubiquitous, and highly conserved pathway leading to the biochemical activation of molybdenum. Moco is the essential component of a group of redox enzymes, which are diverse in terms of their phylogenetic distribution and their architectures, both at the overall level and in their catalytic geometry. A wide variety of transformations are catalyzed by these enzymes at carbon, sulfur and nitrogen atoms, which include the transfer of an oxo group or two electrons to or from the substrate. More than 50 molybdoenzymes were identified in bacteria to date. In molybdoenzymes Mo is coordinated to a dithiolene group on the 6-alkyl side chain of a pterin called molybdopterin (MPT). The biosynthesis of Moco can be divided into four general steps in bacteria: I) formation of the cyclic pyranopterin monophosphate, 2) formation of MPT, 3) insertion of molybdenum into molybdopterin to form Moco, and 4) additional modification of Moco with the attachment of GMP or CMP to the phosphate group of MPT, forming the dinucleotide variant of Moco. This review will focus on molybdoenzymes, the biosynthesis of Moco, and its incorporation into specific target proteins focusing on Escherichia coli. This article is part of a Special Issue entitled: Metals in Bioenergetics and Biomimetics Systems.show moreshow less

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Metadaten
Author:Chantal Iobbi-Nivol, Silke Leimkühler
DOI:https://doi.org/10.1016/j.bbabio.2012.11.007
ISSN:0005-2728 (print)
Parent Title (English):Biochimica et biophysica acta : Bioenergetics
Publisher:Elsevier
Place of publication:Amsterdam
Document Type:Review
Language:English
Year of first Publication:2013
Year of Completion:2013
Release Date:2017/03/26
Tag:Bis-MGD; Dithiolene; Moco; Molybdenum; Molybdenum cofactor; Molybdopterin
Volume:1827
Issue:8-9
Pagenumber:16
First Page:1086
Last Page:1101
Funder:Deutsche Forschungsgemeinschaft; Heisenberg fellowship; CNRS; AMU; DAAD PROCOPE program; Deutsche Forschungsgemeinschaft Cluster of Excellence "Unifying Concepts in Catalysis"
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert