TY  - JOUR
A1  - Mendel, Ralf R.
A1  - Leimkühler, Silke
T1  - The biosynthesis of the molybdenum cofactors
JF  - Journal of biological inorganic chemistry
N2  - The biosynthesis of the molybdenum cofactors (Moco) 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 to date. In all molybdoenzymes except nitrogenase, molybdenum 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 three general steps, with a fourth one present only in bacteria and archaea: (1) 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 in bacteria with the attachment of a nucleotide to the phosphate group of MPT, forming the dinucleotide variant of Moco. This review will focus on the biosynthesis of Moco in bacteria, humans and plants.
KW  - Molybdenum
KW  - Molybdenum cofactor
KW  - cPMP
KW  - bis-MGD
KW  - Sulfuration
KW  - Sulfite oxidase
Y1  - 2015
U6  - https://doi.org/10.1007/s00775-014-1173-y
SN  - 0949-8257
SN  - 1432-1327
VL  - 20
IS  - 2
SP  - 337
EP  - 347
PB  - Springer
CY  - New York
ER  - 
TY  - JOUR
A1  - Frasca, Stefano
A1  - Milan, Anabel Molero
A1  - Guiet, Amandine
A1  - Goebel, Caren
A1  - Perez-Caballero, Fernando
A1  - Stiba, Konstanze
A1  - Leimkühler, Silke
A1  - Fischer, Anna
A1  - Wollenberger, Ursula
T1  - Bioelectrocatalysis at mesoporous antimony doped tin oxide
 electrodes-Electrochemical characterization and direct enzyme
 communication
JF  - ELECTROCHIMICA ACTA
N2  - In this paper we report immobilization and bioelectrocatalysis of human sulfite oxidase (hSO) on nanostructured antimony doped tin oxide (ATO) thin film electrodes. Two types of ATO thin film electrodes were prepared via evaporation induced self-assembly of ATO nanoparticle sols. The use of a porogen results in different porosity and film thickness. Nevertheless both electrode types reveal similar quasi reversible electrochemical behavior for positive and negatively charged small mediators. Facile and durable immobilization of catalytically active enzyme in a direct electron transfer configuration was achieved without further chemical modification of the ATO surfaces. Interestingly, the binding of hSO onto the ATO surface seems to be not only of electrostatic nature, but also originates from a strong interaction between the histidine-tag of the enzyme and the supporting material. This is suggested from stable sulfite dependent bioelectrocatalytic signals at high ionic strength and imidazole desorption experiments. As such, ATO appears as a promising conductive platform for the immobilization of complex enzymes and their application in bioelectrocatalysis. (C) 2013 Elsevier Ltd. All rights reserved.
KW  - Antimony doped tin dioxide
KW  - Sulfite oxidase
KW  - Direct electrochemistry
KW  - Biosensor
KW  - Bioelectrocatalysis
Y1  - 2013
U6  - https://doi.org/10.1016/j.electacta.2013.03.144
SN  - 0013-4686
SN  - 1873-3859
VL  - 110
IS  - 2
SP  - 172
EP  - 180
PB  - PERGAMON-ELSEVIER SCIENCE LTD
CY  - OXFORD
ER  -