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iron-sulfur-molybdenum cofactor biosynthetic process
Known as:
iron-molybdenum cofactor biosynthesis
, iron-molybdenum cofactor biosynthetic process
, FeMo-co formation
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The chemical reactions and pathways resulting in the formation of iron-sulfur-molybdenum cofactor. [GOC:TermGenie, GOC:yaf, UniPathway:UPA00782]
National Institutes of Health
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iron-sulfur-molybdenum cofactor assembly
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
2011
2011
Electronic dimensions of FeMo-co, the active site of nitrogenase, and its catalytic intermediates.
I. Dance
Inorganic Chemistry
2011
Corpus ID: 21560330
The iron-molybdenum cofactor (FeMo-co), which is the catalytic center for the enzymatic conversion of N(2) to NH(3), has the…
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Highly Cited
2006
Highly Cited
2006
Dipyrrolyl precursors to bisalkoxide molybdenum olefin metathesis catalysts.
Adam S. Hock
,
R. Schrock
,
A. Hoveyda
Journal of the American Chemical Society
2006
Corpus ID: 1721334
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…
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2004
2004
Spectroscopic investigation of the nickel-containing porphinoid cofactor F430. Comparison of the free cofactor in the +1, +2 and +3 oxidation states with the cofactor bound to methyl-coenzyme M…
E. Duin
,
L. Signor
,
+6 authors
Michael K. Johnson
JBIC Journal of Biological Inorganic Chemistry
2004
Corpus ID: 19940990
Methyl-coenzyme M reductase (MCR) catalyzes the methane-forming step in methanogenic archaea. It contains the nickel porphinoid…
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Highly Cited
2000
Highly Cited
2000
Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase.
H. Erlandsen
,
E. Bjørgo
,
Torgeir Flatmark
,
Raymond C. Stevens
Biochemistry
2000
Corpus ID: 1060958
The crystal structure of the dimeric catalytic domain (residues 118-424) of human PheOH (hPheOH), cocrystallized with the…
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2000
2000
Stability and activity of alcohol dehydrogenases in W/O-microemulsions: Enantioselective reduction including cofactor regeneration
B. Orlich
,
H. Berger
,
M. Lade
,
R. Schomäcker
2000
Corpus ID: 196590231
Microemulsions provide an interesting alternative to classical methods for the conversion of less water-soluble substrates by…
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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.
Jeffrey T. Bolin
,
Alicia E. Ronco
,
T. Morgan
,
Leonard E. Mortenson
,
N. Xuong
Proceedings of the National Academy of Sciences…
1993
Corpus ID: 27008546
Nitrogenase (EC 1.18.6.1) catalyzes the conversion of dinitrogen to ammonia, the central reaction of biological nitrogen fixation…
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1980
1980
Studies on biologically active pteridines. III. The absolute configuration at the C-6 chiral center of tetrahydrobiopterin cofactor and related compounds.
S. Matsuura
,
T. Sugimoto
,
H. Hasegawa
,
S. Imaizumi
,
A. Ichiyama
Journal of Biochemistry (Tokyo)
1980
Corpus ID: 9020151
Tetrahydrobiopterin, the natural pteridine cofactor for aromatic amino acid hydroxylases, was produced stereopecifically with…
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1979
1979
Identification of iron-sulfur centers in the iron-molybdenum proteins of nitrogenase.
D. Kurtz
,
R. Mcmillan
,
B. Burgess
,
L. Mortenson
,
R. H. Holm
Proceedings of the National Academy of Sciences…
1979
Corpus ID: 40950041
The core extrusion method has been applied to the determination of the type ([2Fe-2S], [4Fe-4S]) and number of iron-sulfur…
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1975
1975
Effects of solvent on the properties of ferredoxins.
R. Cammack
Biochemical Society Transactions
1975
Corpus ID: 27357343
observation temperatures were taken lower. This possibility would be consistent with a suggestion (Massey, 1973) that aldehyde…
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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
P. Batist
,
C. J. Kapteijns
,
B. C. Lippens
,
G. Schuit
1967
Corpus ID: 94179976
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