Homocitrate is a component of the iron-molybdenum cofactor of nitrogenase

When apodinitrogenase (lacking FeMo-co) was activated with FeMo-co synthesized in vitro in the presence of 3H-labeled homocitrate, label was incorporated into dinitrogenase. The physical association of the label with FeMo-co was demonstrated by reisolation and purification of the cofactor from dinit...

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Published inBiochemistry (Easton) Vol. 28; no. 7; pp. 2768 - 2771
Main Authors Hoover, Timothy R, Imperial, Juan, Ludden, Paul W, Shah, Vinod K
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 04.04.1989
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Abstract When apodinitrogenase (lacking FeMo-co) was activated with FeMo-co synthesized in vitro in the presence of 3H-labeled homocitrate, label was incorporated into dinitrogenase. The physical association of the label with FeMo-co was demonstrated by reisolation and purification of the cofactor from dinitrogenase. The presence of homocitrate in FeMo-co was established by NMR analysis of the organic acid extracted from dinitrogenase. Quantitation of homocitrate in dinitrogenase showed it to be present at a 1:1 ratio with molybdenum.
AbstractList When apodinitrogenase (lacking FeMo-co) was activated with FeMo-co synthesized in vitro in the presence of 3H-labeled homocitrate, label was incorporated into dinitrogenase. The physical association of the label with FeMo-co was demonstrated by reisolation and purification of the cofactor from dinitrogenase. The presence of homocitrate in FeMo-co was established by NMR analysis of the organic acid extracted from dinitrogenase. Quantitation of homocitrate in dinitrogenase showed it to be present at a 1:1 ratio with molybdenum.
When apodinitrogenase (lacking FeMo-co) was activated with FeMo-co synthesized in vitro in the presence of {sup 3}H-labeled homocitrate, label was incorporated into dinitrogenase. The physical association of he label with FeMo-co was demonstrated by reisolation and purification of the cofactor from dinitrogenase. The presence of homocitrate in FeMo-co was established by NMR analysis of the organic acid extracted from dinitrogenase. Quantitation of homocitrate in dinitrogenase showed it to be present at 1:1 ratio with molybdenum.
Author Imperial, Juan
Shah, Vinod K
Hoover, Timothy R
Ludden, Paul W
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/2663059$$D View this record in MEDLINE/PubMed
https://www.osti.gov/biblio/5673222$$D View this record in Osti.gov
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Snippet When apodinitrogenase (lacking FeMo-co) was activated with FeMo-co synthesized in vitro in the presence of 3H-labeled homocitrate, label was incorporated into...
When apodinitrogenase (lacking FeMo-co) was activated with FeMo-co synthesized in vitro in the presence of {sup 3}H-labeled homocitrate, label was incorporated...
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SubjectTerms 550201 - Biochemistry- Tracer Techniques
BASIC BIOLOGICAL SCIENCES
BIOSYNTHESIS
CARBOXYLIC ACID SALTS
Chromatography, DEAE-Cellulose
Chromatography, Gel
Chromatography, Ion Exchange
CITRATES
COENZYMES
ENZYMES
Ferredoxins - biosynthesis
HYDROGEN COMPOUNDS
Kinetics
Klebsiella pneumoniae - enzymology
MAGNETIC RESONANCE
Magnetic Resonance Spectroscopy
Molybdoferredoxin - biosynthesis
Molybdoferredoxin - isolation & purification
NITRO-GROUP DEHYDROGENASES
NITROGENASE
Nitrogenase - biosynthesis
Nitrogenase - isolation & purification
NUCLEAR MAGNETIC RESONANCE
OXIDOREDUCTASES
PURIFICATION
RESONANCE
SYNTHESIS
Tricarboxylic Acids - analysis
Tricarboxylic Acids - metabolism
TRITIUM COMPOUNDS
UPTAKE
Title Homocitrate is a component of the iron-molybdenum cofactor of nitrogenase
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Volume 28
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