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Literature summary for 1.18.6.1 extracted from

  • Mayweather, D.; Danyal, K.; Dean, D.R.; Seefeldt, L.C.; Hoffman, B.M.
    Temperature invariance of the nitrogenase electron transfer mechanism (2012), Biochemistry, 51, 8391-8398.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.18.6.1

Organism

Organism UniProt Comment Textmining
Azotobacter vinelandii
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Azotobacter vinelandii DJ995
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information using buffer 3-(N-morpholino)propanesulfonic acid, which has a very small temperature coefficient, temperature-dependent elctron transfer rate constants are observed, with nonlinear Arrhenius plots and with electron transfers gated across the temperature range by a conformational change that involves the binding of numerous water molecules, consistent with an unchanging electron transfer mechanism. There is no solvent kinetic isotope effect throughout the temperature range studied, consistent with an unchanging mechanismn. The nonlinear Arrhenius plots are explained by the change in heat capacity caused by the binding of water molecules in an invariant gating electron transfer mechanism. The observations contradict the idea of a change in electron transfer mechanism with cooling Azotobacter vinelandii ?
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additional information using buffer 3-(N-morpholino)propanesulfonic acid, which has a very small temperature coefficient, temperature-dependent elctron transfer rate constants are observed, with nonlinear Arrhenius plots and with electron transfers gated across the temperature range by a conformational change that involves the binding of numerous water molecules, consistent with an unchanging electron transfer mechanism. There is no solvent kinetic isotope effect throughout the temperature range studied, consistent with an unchanging mechanismn. The nonlinear Arrhenius plots are explained by the change in heat capacity caused by the binding of water molecules in an invariant gating electron transfer mechanism. The observations contradict the idea of a change in electron transfer mechanism with cooling Azotobacter vinelandii DJ995 ?
-
 ?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
additional information
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 using buffer 3-(N-morpholino)propanesulfonic acid, which has a very small temperature coefficient, temperature-dependent elctron transfer rate constants are observed, with nonlinear Arrhenius plots and with electron transfers gated across the temperature range by a conformational change that involves the binding of numerous water molecules, consistent with an unchanging electron transfer mechanism. There is no solvent kinetic isotope effect throughout the temperature range studied, consistent with an unchanging mechanismn. The nonlinear Arrhenius plots are explained by the change in heat capacity caused by the binding of water molecules in an invariant gating electron transfer mechanism. The observations contradict the idea of a change in electron transfer mechanism with cooling Azotobacter vinelandii