Skip to search formSkip to main contentSkip to account menu

iron-sulfur-molybdenum cofactor biosynthetic process

Known as: iron-molybdenum cofactor biosynthesis, iron-molybdenum cofactor biosynthetic process, FeMo-co formation 
The chemical reactions and pathways resulting in the formation of iron-sulfur-molybdenum cofactor. [GOC:TermGenie, GOC:yaf, UniPathway:UPA00782]
National Institutes of Health

Related topics

Related topics

1 relation
iron-sulfur-molybdenum cofactor assembly

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2012
Review
2012
The glmS ribozyme cofactor is a general acid-base catalyst.
The glmS ribozyme is the first natural self-cleaving ribozyme known to require a cofactor. The d-glucosamine-6-phosphate (GlcN6P… 
Highly Cited
2011
Highly Cited
2011
Reversible heme-dependent regulation of human cystathionine β-synthase by a flavoprotein oxidoreductase.
Human CBS is a PLP-dependent enzyme that clears homocysteine, gates the flow of sulfur into glutathione, and contributes to the… 
Highly Cited
2006
Highly Cited
2006
Gas chromatography on self-assembled, single-walled carbon nanotubes.
High-performance stationary phases, which provide high resolutions and are stable at high temperatures, are of significant… 
Highly Cited
2006
Highly Cited
2006
Dipyrrolyl precursors to bisalkoxide molybdenum olefin metathesis catalysts.
Addition of 2 equiv of lithium pyrrolide to Mo(NR)(CHCMe2R')(OTf)2(DME) (OTf = OSO2CF3; R = 2,6-i-Pr2C6H3, 1-adamantyl, or 2,6… 
2003
2003
An amperometric bi-enzyme sensor for determination of formate using cofactor regeneration.
Highly Cited
2000
Highly Cited
2000
Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase.
The crystal structure of the dimeric catalytic domain (residues 118-424) of human PheOH (hPheOH), cocrystallized with the… 
Highly Cited
1993
Highly Cited
1993
The unusual metal clusters of nitrogenase: structural features revealed by x-ray anomalous diffraction studies of the MoFe protein from Clostridium pasteurianum.
Nitrogenase (EC 1.18.6.1) catalyzes the conversion of dinitrogen to ammonia, the central reaction of biological nitrogen fixation… 
1979
1979
Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.
The core extrusion method has been applied to the determination of the type ([2Fe-2S], [4Fe-4S]) and number of iron-sulfur… 
Highly Cited
1968
Highly Cited
1968
Carbonyl halides of the Group VI transition metals. V. Carbon monoxide carriers and some sulphur and nitrogen derivatives of molybdenum halocarbonyls
The blue compounds MX2(CO)2(Ph3P)2 (M = Mo and W, X = Cl and Br) have been shown to absorb carbon monoxide very readily indeed to… 
Highly Cited
1967
Highly Cited
1967
Catalytic oxidation of 1-butene over bismuth molybdate catalysts : III. Reduction of bismuth oxide, molybdenum oxide, bismuth molybdate, and of some nonstoichiometric molybdenum oxides with 1-butene
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)