TY  - JOUR
A1  - Yokoyama, Kenichi
A1  - Leimkühler, Silke
T1  - The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria
T2  - Biochimica et biophysica acta : Molecular cell research
N2  - The biosynthesis of the molybdenum cofactor (Moco) has been intensively studied, in addition to its insertion into molybdoenzymes. In particular, a link between the assembly of molybdoenzymes and the biosynthesis of FeS clusters has been identified in the recent years: 1) the synthesis of the first intermediate in Moco biosynthesis requires an FeS-cluster containing protein, 2) the sulfurtransferase for the dithiolene group in Moco is also involved in the synthesis of FeS clusters, thiamin and thiolated tRNAs, 3) the addition of a sulfido-ligand to the molybdenum atom in the active site additionally involves a sulfurtransferase, and 4) most molybdoenzymes in bacteria require FeS clusters as redox active cofactors. In this review we will focus on the biosynthesis of the molybdenum cofactor in bacteria, its modification and insertion into molybdoenzymes, with an emphasis to its link to FeS cluster biosynthesis and sulfur transfer. (C) 2014 Elsevier B.V. All rights reserved.
KW  - Molybdenum-iron-iron-sulfur cluster
KW  - Molybdenum cofactor
KW  - tRNA
KW  - Sulfur transfer
KW  - L-Cysteine desulfurase
Y1  - 2015
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/38896
SN  - 0167-4889
SN  - 0006-3002
VL  - 1853
IS  - 6
SP  - 1335
EP  - 1349
PB  - Elsevier
CY  - Amsterdam
ER  -