Results 1 to 10 of about 70 (63)
Incorporation of Molybdenum into the Iron-Molybdenum Cofactor of Nitrogenase [PDF]
Journal of Biological Chemistry, 1999 The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of dinitrogenase was investigated using 99Mo to follow the incorporation of Mo into precursors. 99Mo label accumulates on dinitrogenase only when all known components of the FeMo-co synthesis system, NifH, NifNE, NifB-cofactor, homocitrate, MgATP, and reductant, are present.
R M, Allen +5 more
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Journal of Biological Chemistry, 2013 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.
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Molybdenum Cofactor Deficiency in Humans
Molecules, 2022 Molybdenum cofactor (Moco) deficiency (MoCD) is characterized by neonatal-onset myoclonic epileptic encephalopathy and dystonia with cerebral MRI changes similar to hypoxic–ischemic lesions. The molecular cause of the disease is the loss of sulfite oxidase (SOX) activity, one of four Moco-dependent enzymes in men.
Lena Johannes +2 more
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Biology of the molybdenum cofactor [PDF]
Journal of Experimental Botany, 2007 The transition element molybdenum (Mo) is an essential micronutrient for plants where it is needed as a catalytically active metal during enzyme catalysis. Four plant enzymes depend on molybdenum: nitrate reductase, sulphite oxidase, xanthine dehydrogenase, and aldehyde oxidase.
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Molybdoenzymes and molybdenum cofactor in plants [PDF]
Journal of Experimental Botany, 2002 The transition element molybdenum (Mo) is essential for (nearly) all organisms and occurs in more than 40 enzymes catalysing diverse redox reactions, however, only four of them have been found in plants. (1) Nitrate reductase catalyses the key step in inorganic nitrogen assimilation, (2) aldehyde oxidase(s) have been shown to catalyse the last step in ...
Ralf R, Mendel, Robert, Hänsch
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A crystallographic view of the molybdenum cofactor † [PDF]
Journal of the Chemical Society, Dalton Transactions, 1997 The molybdenum cofactor (Moco) has been found to be associated with a diverse set of redox enzymes and contains a mononuclear molybdenum or tungsten ion co-ordinated by the dithiolene sulfurs of one or two molybdopterin {a pterin [2-amino-4(1H)-pteridinone] derivative} ligands.
Rees, Douglas C. +3 more
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Molybdenum cofactor deficiency [PDF]
, 2020 Molybdenum cofactor (MoCo) deficiency presents classically in the neonatal period, with convulsions intractable to anticonvulsant therapy and coma. The clinical manifestations of MoCo deficiency relating to the nervous system are generally considered to be functions of the deficiency of sulfite oxidase.
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Biosynthesis of the iron-molybdenum cofactor and the molybdenum cofactor in Klebsiella pneumoniae: effect of sulfur source [PDF]
Journal of Bacteriology, 1985 NifQ- and Mol- mutants of Klebsiella pneumoniae show an elevated molybdenum requirement for nitrogen fixation. Substitution of cystine for sulfate as the sulfur source in the medium reduced the molybdenum requirement of these mutants to levels required by the wild type.
R A, Ugalde +3 more
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The pterin molybdenum cofactors.
Journal of Biological Chemistry, 1992 crassa, demonstrated that the inactive apoprotein of nitrate reductase in extracts of the mutant could be reconstituted by the addition of denatured preparations of purified molybdoenzymes from animal, fungal, or bacterial origin. This crucial finding showed that mol- ybdoenzymes contain a dissociable entity fitting the description of a cofactor and ...
K V, Rajagopalan, J L, Johnson
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Molybdenum Cofactor Biosynthesis [PDF]
Journal of Biological Chemistry, 1997 Günter Schwarz +2 more
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