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Vanadium nitrogenase information


Azotobacter sp. cells, stained with Heidenhain's iron hematoxylin, ×1000. Vanadium Nitrogenases are found in members of the bacteria genus Azotobacter as well as the species R. palustris and A. variabilis[1][2]

Vanadium nitrogenase is a key enzyme for nitrogen fixation found in nitrogen-fixing bacteria, and is used as an alternative to molybdenum nitrogenase when molybdenum is unavailable.[1] Vanadium nitrogenases are an important biological use of vanadium, which is uncommonly used by life. An important component of the nitrogen cycle, vanadium nitrogenase converts nitrogen gas to ammonia, thereby making otherwise inaccessible nitrogen available to plants. Unlike molybdenum nitrogenase, vanadium nitrogenase can also reduce carbon monoxide to ethylene, ethane and propane[3] but both enzymes can reduce protons to hydrogen gas and acetylene to ethylene.

  1. ^ a b Rehder D. (2000). "Vanadium Nitrogenase". Journal of Inorganic Biochemistry. 80 (1–2): 133–6. doi:10.1016/S0162-0134(00)00049-0. PMID 10885473.
  2. ^ Larimer; et al. (2004). "Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris". Nature Biotechnology. 22 (1): 55–61. doi:10.1038/nbt923. PMID 14704707.
  3. ^ Hadlington S. "Nitrogenase Found to be a Two-Trick Pony". Royal Society of Chemistry. Retrieved 2010-08-05.

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Vanadium nitrogenase

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Vanadium nitrogenase is a key enzyme for nitrogen fixation found in nitrogen-fixing bacteria, and is used as an alternative to molybdenum nitrogenase...

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Nitrogenase

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types of nitrogenase found in various nitrogen-fixing bacteria: molybdenum (Mo) nitrogenase, vanadium (V) nitrogenase, and iron-only (Fe) nitrogenase. Molybdenum...

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Vanadium

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R-Br + H2O + OH− A vanadium nitrogenase is used by some nitrogen-fixing micro-organisms, such as Azotobacter. In this role, vanadium serves in place of...

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Diazotroph

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and Azospirillum. All diazotrophs contain iron-molybdenum or iron-vanadium nitrogenase systems. Two of the most studied systems are those of Klebsiella...

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Azotobacter

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(1988). "Molybdenum and vanadium nitrogenases of Azotobacter chroococcum. Low temperature favours N2 reduction by vanadium nitrogenase". Biochemical Journal...

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Nitrogen fixation

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molybdenum-dependent nitrogenase, followed by closely related nitrogenase reductases (component II) vnfH and anfH representing vanadium-dependent and iron-only...

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Vanadium cycle

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in alternative nitrogenases. Schlesinger, William H.; Klein, Emily M.; Vengosh, Avner (2017). "Global biogeochemical cycle of vanadium". Proceedings of...

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Molybdenum

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is a component in most nitrogenases. Among molybdoenzymes, nitrogenases are unique in lacking the molybdopterin. Nitrogenases catalyze the production...

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Serena DeBeer

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to identify the central carbon atom in FeMo cofactor of Nitrogenase (see section Nitrogenase). The DeBeer group is actively involved in the development...

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Noris Salazar Allen

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"Complete genomes of symbiotic cyanobacteria clarify the evolution of vanadium-nitrogenase." Genome biology and evolution 11.7 (2019): 1959-1964. Horwath, Aline...

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Trimesitylvanadium

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Mes = 2,4,6-trimethylphenyl) is one of the organovanadium complexes with vanadium in an oxidation state of 3. This compound was first synthesized by W. Seidel...

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Transition metal oxo complex

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their synthetic chemistry, and also in their biological role (aside from nitrogenase). The biologically transported species and starting point for biosynthesis...

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Rhodopseudomonas palustris

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palustris has the unique characteristic of encoding for a vanadium-containing nitrogenase. It produces, as a byproduct of nitrogen fixation, three times...

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Metalloprotein

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pp. 257. ISBN 9780841227088. Chan MK, Kim J, Rees DC (May 1993). "The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures". Science...

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Hemoglobin

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containing oxygen-binding protein. The specific enzyme protected is nitrogenase, which is unable to reduce nitrogen gas in the presence of free oxygen...

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Nitrogen cycle

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by the activity of molybdenum (Mo)-nitrogenase, found in a wide variety of bacteria and some Archaea. Mo-nitrogenase is a complex two-component enzyme...

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Plant nutrition

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nitrate reductase enzyme (needed for the reduction of nitrate) and the nitrogenase enzyme (required for biological nitrogen fixation). Reduced productivity...

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Evolution of metal ions in biological systems

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the reduction of dinitrogen to ammonia, which occurs in one type of nitrogenases. These enzymes are used by bacteria that usually live in a symbiotic...

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Transition metal dinitrogen complex

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probably occurs via the binding of N2 to those metal centers in the enzyme nitrogenase, followed by a series of steps that involve electron transfer and protonation...

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Julie Kovacs

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synthesis of iron-sulfur cluster compounds, which mimic the FeMo-cofactor of nitrogenase. She then moved to Harvard University for graduate studies, and there...

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Iron cycle

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component of hemoglobin, important to nitrogen fixation as part of the Nitrogenase enzyme family, and as part of the iron-sulfur core of ferredoxin it facilitates...

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Sulfur

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which serve as electron shuttles in cells. In bacteria, the important nitrogenase enzymes contain an Fe–Mo–S cluster and is a catalyst that performs the...

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Iron

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required for life. The iron–sulfur clusters are pervasive and include nitrogenase, the enzymes responsible for biological nitrogen fixation. Iron-containing...

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Nitrogen

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central metal cation, illustrate how N2 might bind to the metal(s) in nitrogenase and the catalyst for the Haber process: these processes involving dinitrogen...

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