» Articles » PMID: 3223922

Molybdenum and Vanadium Nitrogenases of Azotobacter Chroococcum. Low Temperature Favours N2 Reduction by Vanadium Nitrogenase

Overview
Journal Biochem J
Specialty Biochemistry
Date 1988 Dec 1
PMID 3223922
Citations 31
Authors
Affiliations
Soon will be listed here.
Abstract

A comparison of the effect of temperature on the reduction of N2 by purified molybdenum nitrogenase and vanadium nitrogenase of Azotobacter chroococcum showed differences in behaviour. As the assay temperature was lowered from 30 degrees C to 5 degrees C N2 remained an effective substrate for V nitrogenase, but not Mo nitrogenase, since the specific activity for N2 reduction by Mo nitrogenase decreased 10-fold more than that of V nitrogenase. Activity cross-reactions between nitrogenase components showed the enhanced low-temperature activity to be associated with the Fe protein of V nitrogenase. The lower activity of homologous Mo nitrogenase components, although dependent on the ratio of MoFe protein to Fe protein, did not equal that of V nitrogenase even under conditions of high electron flux obtained at a 12-fold molar excess of Fe protein.

Citing Articles

Characterizing the Interplay of Rubisco and Nitrogenase Enzymes in Anaerobic-Photoheterotrophically Grown Rhodopseudomonas palustris CGA009 through a Genome-Scale Metabolic and Expression Model.

Chowdhury N, Alsiyabi A, Saha R Microbiol Spectr. 2022; 10(4):e0146322.

PMID: 35730964 PMC: 9431616. DOI: 10.1128/spectrum.01463-22.


Influence of Mo and Fe on Photosynthetic and Nitrogenase Activities of Nitrogen-Fixing Cyanobacteria under Nitrogen Starvation.

Sadvakasova A, Kossalbayev B, Token A, Bauenova M, Wang J, Zayadan B Cells. 2022; 11(5).

PMID: 35269526 PMC: 8909559. DOI: 10.3390/cells11050904.


Expression, Isolation, and Characterization of Vanadium Nitrogenase from Azotobacter vinelandii.

Parison K, Gies-Elterlein J, Trncik C, Einsle O Methods Mol Biol. 2021; 2353:97-121.

PMID: 34292546 DOI: 10.1007/978-1-0716-1605-5_6.


Radiation of nitrogen-metabolizing enzymes across the tree of life tracks environmental transitions in Earth history.

Parsons C, Stueken E, Rosen C, Mateos K, Anderson R Geobiology. 2020; 19(1):18-34.

PMID: 33108025 PMC: 7894544. DOI: 10.1111/gbi.12419.


Quantum Mechanics/Molecular Mechanics Study of Resting-State Vanadium Nitrogenase: Molecular and Electronic Structure of the Iron-Vanadium Cofactor.

Benediktsson B, Bjornsson R Inorg Chem. 2020; 59(16):11514-11527.

PMID: 32799489 PMC: 7458435. DOI: 10.1021/acs.inorgchem.0c01320.


References
1.
Dilworth M, Eady R, Eldridge M . The vanadium nitrogenase of Azotobacter chroococcum. Reduction of acetylene and ethylene to ethane. Biochem J. 1988; 249(3):745-51. PMC: 1148769. DOI: 10.1042/bj2490745. View

2.
Eady R, Robson R, Richardson T, Miller R, Hawkins M . The vanadium nitrogenase of Azotobacter chroococcum. Purification and properties of the VFe protein. Biochem J. 1987; 244(1):197-207. PMC: 1147972. DOI: 10.1042/bj2440197. View

3.
Hales B, Case E, Morningstar J, Dzeda M, Mauterer L . Isolation of a new vanadium-containing nitrogenase from Azotobacter vinelandii. Biochemistry. 1986; 25(23):7251-5. DOI: 10.1021/bi00371a001. View

4.
Bishop P, Jarlenski D, Hetherington D . Evidence for an alternative nitrogen fixation system in Azotobacter vinelandii. Proc Natl Acad Sci U S A. 1980; 77(12):7342-6. PMC: 350499. DOI: 10.1073/pnas.77.12.7342. View

5.
Hales B, Langosch D, Case E . Isolation and characterization of a second nitrogenase Fe-protein from Azotobacter vinelandii. J Biol Chem. 1986; 261(32):15301-6. View