Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate

T. R. Hoover, A. D. Robertson, Ronald Cerny, R. N. Hayes, J. Imperial, V. K. Shah, P. W. Ludden

Research output: Contribution to journalArticle

91 Citations (Scopus)

Abstract

Nitrogenase catalyses the ATP-dependent reduction of N 2 to NH 3 , and is composed of two proteins, dinitrogenase (MoFe protein or component I) and dinitrogenase reductase (Fe protein or component II) 1,2 . Dinitrogenase contains a unique prosthetic group (iron-molybdenum cofactor, FeMoco) comprised of Fe, Mo and S, which has been proposed as the site of N 2 reduction 3-5 . Biochemical and genetic studies of Nif - (nitrogen fixation) mutants of Klebsiella pneumoniae which are defective in nitrogen fixation, have shown that the nifB, nifQ, nifN, nifE and nifV genes are required for the biosynthesis of FeMo-co 5-7 . Recently, a system for in vitro synthesis of FeMoco was described 8 . The assay requires at least the nifB, nifN and nifE gene products 8 , and a low-molecular-weight factor (V factor) produced in the presence of the nifV gene product 9 . We have used this system to study FeMoco biosynthesis. We report here the isolation of V factor and identify it as homocitric acid ([R]2-hydroxy-l,2,4-butanetricarboxylic acid).

Original languageEnglish (US)
Pages (from-to)855-857
Number of pages3
JournalNature
Volume329
Issue number6142
DOIs
StatePublished - Jan 1 1987

Fingerprint

Molybdoferredoxin
Nitrogenase
Nitrogen Fixation
Dinitrogenase Reductase
Genes
Factor V
Klebsiella pneumoniae
Molecular Biology
Proteins
Adenosine Triphosphate
Molecular Weight
Acids
homocitric acid

ASJC Scopus subject areas

  • General

Cite this

Hoover, T. R., Robertson, A. D., Cerny, R., Hayes, R. N., Imperial, J., Shah, V. K., & Ludden, P. W. (1987). Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate. Nature, 329(6142), 855-857. https://doi.org/10.1038/329855a0

Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate. / Hoover, T. R.; Robertson, A. D.; Cerny, Ronald; Hayes, R. N.; Imperial, J.; Shah, V. K.; Ludden, P. W.

In: Nature, Vol. 329, No. 6142, 01.01.1987, p. 855-857.

Research output: Contribution to journalArticle

Hoover, TR, Robertson, AD, Cerny, R, Hayes, RN, Imperial, J, Shah, VK & Ludden, PW 1987, 'Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate', Nature, vol. 329, no. 6142, pp. 855-857. https://doi.org/10.1038/329855a0
Hoover, T. R. ; Robertson, A. D. ; Cerny, Ronald ; Hayes, R. N. ; Imperial, J. ; Shah, V. K. ; Ludden, P. W. / Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate. In: Nature. 1987 ; Vol. 329, No. 6142. pp. 855-857.
@article{b92626ea0eae47bd93cd95ff9f3140c3,
title = "Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate",
abstract = "Nitrogenase catalyses the ATP-dependent reduction of N 2 to NH 3 , and is composed of two proteins, dinitrogenase (MoFe protein or component I) and dinitrogenase reductase (Fe protein or component II) 1,2 . Dinitrogenase contains a unique prosthetic group (iron-molybdenum cofactor, FeMoco) comprised of Fe, Mo and S, which has been proposed as the site of N 2 reduction 3-5 . Biochemical and genetic studies of Nif - (nitrogen fixation) mutants of Klebsiella pneumoniae which are defective in nitrogen fixation, have shown that the nifB, nifQ, nifN, nifE and nifV genes are required for the biosynthesis of FeMo-co 5-7 . Recently, a system for in vitro synthesis of FeMoco was described 8 . The assay requires at least the nifB, nifN and nifE gene products 8 , and a low-molecular-weight factor (V factor) produced in the presence of the nifV gene product 9 . We have used this system to study FeMoco biosynthesis. We report here the isolation of V factor and identify it as homocitric acid ([R]2-hydroxy-l,2,4-butanetricarboxylic acid).",
author = "Hoover, {T. R.} and Robertson, {A. D.} and Ronald Cerny and Hayes, {R. N.} and J. Imperial and Shah, {V. K.} and Ludden, {P. W.}",
year = "1987",
month = "1",
day = "1",
doi = "10.1038/329855a0",
language = "English (US)",
volume = "329",
pages = "855--857",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6142",

}

TY - JOUR

T1 - Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate

AU - Hoover, T. R.

AU - Robertson, A. D.

AU - Cerny, Ronald

AU - Hayes, R. N.

AU - Imperial, J.

AU - Shah, V. K.

AU - Ludden, P. W.

PY - 1987/1/1

Y1 - 1987/1/1

N2 - Nitrogenase catalyses the ATP-dependent reduction of N 2 to NH 3 , and is composed of two proteins, dinitrogenase (MoFe protein or component I) and dinitrogenase reductase (Fe protein or component II) 1,2 . Dinitrogenase contains a unique prosthetic group (iron-molybdenum cofactor, FeMoco) comprised of Fe, Mo and S, which has been proposed as the site of N 2 reduction 3-5 . Biochemical and genetic studies of Nif - (nitrogen fixation) mutants of Klebsiella pneumoniae which are defective in nitrogen fixation, have shown that the nifB, nifQ, nifN, nifE and nifV genes are required for the biosynthesis of FeMo-co 5-7 . Recently, a system for in vitro synthesis of FeMoco was described 8 . The assay requires at least the nifB, nifN and nifE gene products 8 , and a low-molecular-weight factor (V factor) produced in the presence of the nifV gene product 9 . We have used this system to study FeMoco biosynthesis. We report here the isolation of V factor and identify it as homocitric acid ([R]2-hydroxy-l,2,4-butanetricarboxylic acid).

AB - Nitrogenase catalyses the ATP-dependent reduction of N 2 to NH 3 , and is composed of two proteins, dinitrogenase (MoFe protein or component I) and dinitrogenase reductase (Fe protein or component II) 1,2 . Dinitrogenase contains a unique prosthetic group (iron-molybdenum cofactor, FeMoco) comprised of Fe, Mo and S, which has been proposed as the site of N 2 reduction 3-5 . Biochemical and genetic studies of Nif - (nitrogen fixation) mutants of Klebsiella pneumoniae which are defective in nitrogen fixation, have shown that the nifB, nifQ, nifN, nifE and nifV genes are required for the biosynthesis of FeMo-co 5-7 . Recently, a system for in vitro synthesis of FeMoco was described 8 . The assay requires at least the nifB, nifN and nifE gene products 8 , and a low-molecular-weight factor (V factor) produced in the presence of the nifV gene product 9 . We have used this system to study FeMoco biosynthesis. We report here the isolation of V factor and identify it as homocitric acid ([R]2-hydroxy-l,2,4-butanetricarboxylic acid).

UR - http://www.scopus.com/inward/record.url?scp=0023616333&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023616333&partnerID=8YFLogxK

U2 - 10.1038/329855a0

DO - 10.1038/329855a0

M3 - Article

C2 - 3313054

AN - SCOPUS:0023616333

VL - 329

SP - 855

EP - 857

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6142

ER -