3FCJ

Nitroalkane oxidase: mutant402N crystallized with nitroethane

3FCJ の概要

• エントリーDOI: 10.2210/pdb3fcj/pdb
• 分子名称: Nitroalkane oxidase, FLAVIN-ADENINE DINUCLEOTIDE, nitroethane, ... (5 entities in total)
• 機能のキーワード: oxidoreductase flavoenzyme, nitroalkane, acyl-coa dehydrogenase, fad, substrate complex, flavoprotein, oxidoreductase
• 由来する生物種: Fusarium oxysporum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 196343.30

構造登録者

Major, D.T.,Gao, J.,Heroux, A.,Orville, A.M.,Valley, M.P.,Fitzpatrick, P.F. (登録日: 2008-11-21, 公開日: 2009-11-03, 最終更新日: 2023-12-27)

主引用文献

Major, D.T.,Heroux, A.,Orville, A.M.,Valley, M.P.,Fitzpatrick, P.F.,Gao, J.
Differential quantum tunneling contributions in nitroalkane oxidase catalyzed and the uncatalyzed proton transfer reaction.
Proc.Natl.Acad.Sci.USA, 106:20734-20739, 2009

PubMed Abstract: The proton transfer reaction between the substrate nitroethane and Asp-402 catalyzed by nitroalkane oxidase and the uncatalyzed process in water have been investigated using a path-integral free-energy perturbation method. Although the dominating effect in rate acceleration by the enzyme is the lowering of the quasiclassical free energy barrier, nuclear quantum effects also contribute to catalysis in nitroalkane oxidase. In particular, the overall nuclear quantum effects have greater contributions to lowering the classical barrier in the enzyme, and there is a larger difference in quantum effects between proton and deuteron transfer for the enzymatic reaction than that in water. Both experiment and computation show that primary KIEs are enhanced in the enzyme, and the computed Swain-Schaad exponent for the enzymatic reaction is exacerbated relative to that in the absence of the enzyme. In addition, the computed tunneling transmission coefficient is approximately three times greater for the enzyme reaction than the uncatalyzed reaction, and the origin of the difference may be attributed to a narrowing effect in the effective potentials for tunneling in the enzyme than that in aqueous solution.

PubMed: 19926855
DOI: 10.1073/pnas.0911416106

実験手法

X-RAY DIFFRACTION (2.4 Å)