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J Biol Chem. 2013 May 10;288(19):13165-72. doi: 10.1074/jbc.R113.455311. Epub 2013 Mar 28.

The molybdenum cofactor.

Author information

1
Department of Plant Biology, Braunschweig University of Technology, 38106 Braunschweig, Germany. r.mendel@tu-bs.de

Abstract

The transition element molybdenum needs to be complexed by a special cofactor to gain catalytic activity. Molybdenum is bound to a unique pterin, thus forming the molybdenum cofactor (Moco), which, in different variants, is the active compound at the catalytic site of all molybdenum-containing enzymes in nature, except bacterial molybdenum nitrogenase. The biosynthesis of Moco involves the complex interaction of six proteins and is a process of four steps, which also require iron, ATP, and copper. After its synthesis, Moco is distributed, involving Moco-binding proteins. A deficiency in the biosynthesis of Moco has lethal consequences for the respective organisms.

KEYWORDS:

Iron; Metalloenzymes; Metalloproteins; Metals; Molybdenum

PMID:
23539623
PMCID:
PMC3650355
DOI:
10.1074/jbc.R113.455311
[Indexed for MEDLINE]
Free PMC Article

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