3FCJ
Nitroalkane oxidase: mutant402N crystallized with nitroethane
Summary for 3FCJ
| Entry DOI | 10.2210/pdb3fcj/pdb |
| Descriptor | Nitroalkane oxidase, FLAVIN-ADENINE DINUCLEOTIDE, nitroethane, ... (5 entities in total) |
| Functional Keywords | oxidoreductase flavoenzyme, nitroalkane, acyl-coa dehydrogenase, fad, substrate complex, flavoprotein, oxidoreductase |
| Biological source | Fusarium oxysporum |
| Total number of polymer chains | 4 |
| Total formula weight | 196343.30 |
| Authors | Major, D.T.,Gao, J.,Heroux, A.,Orville, A.M.,Valley, M.P.,Fitzpatrick, P.F. (deposition date: 2008-11-21, release date: 2009-11-03, Last modification date: 2023-12-27) |
| Primary citation | 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 Cited by 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: 19926855DOI: 10.1073/pnas.0911416106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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