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KL Britton HF Rogers Y Asano T Dairi Y Kato TJ Stillman DW Rice 《Acta crystallographica. Section D, Biological crystallography》1998,53(4):124-126
The novel NAD+-linked opine dehydrogenase from a soil isolate Arthrobacter sp. strain 1C belongs to an enzyme superfamily whose members exhibit quite diverse substrate specificites. Crystals of this opine dehydrogenase, obtained in the presence or absence of co-factor and substrates, have been shown to diffract to beyond 1.8 ? resolution. X-ray precession photographs have established that the crystals belong to space group P21212, with cell parameters a = 104.9, b = 80.0, c = 45.5 ? and a single subunit in the asymmetric unit. The elucidation of the three-dimensional structure of this enzyme will provide a structural framework for this novel class of dehydrogenases to enable a comparison to be made with other enzyme families and also as the basis for mutagenesis experiments directed towards the production of natural and synthetic opine-type compounds containing two chiral centres. 相似文献
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J. Telser H. -I. Lee E. T. Smith H. Huang P. Brereton M. W. W. Adams R. C. Conover M. K. Johnson B. M. Hoffman 《Applied magnetic resonance》1998,14(2-3):305-321
The hyperthermophilic archaeonPyrococcus furiosus contains a four-Fe ferredoxin (Pf- Fd) that differs from most other 4Fe-Fd’s in that its [Fe4S4] cluster is anchored to protein by only three cysteinyl residues.Pf- Fd also is of interest because in its reduced form, [Fe4S4]+, the cluster exhibits bothS = 1/2 andS = 3/2 spin states. Addition of excess cyanide ion converts the cluster exclusively to anS = 1/2 state (g1 = 2.09, g2 = 1.95, g3 = 1.92), however dialysis restores the EPR signal of native reduced protein indicating that the cluster is not irreversibly altered by cyanide. Both the native protein and protein in the presence of excess cyanide ion (Pf- Fd 4Fe-CN) were investigated here using the techniques of electron paramagnetic resonance (EPR) and electron-nuclear double resonance (ENDOR) spectroscopy. In particular,Pf- Fd 4Fe-CN was investigated using13CN? and C15N? ligands.13C and15N ENDOR indicated that a single cyanide ion bound directly, with the cluster showing an unusually small contact interaction (aiso(13C)~ ?3 MHz, aiso(15N) ~ 0). This is in contrast to cyanide bound to monomeric low-spin Fe(III)-containing proteins such as transferrin and myoglobin, for which the13C hyperfine coupling has a large isotropic component (aiso(13C) ≈ ?30 MHz). This small contact interaction is not due to low spin density of Fe, as57Fe ENDOR of the singly and triply labeledPf- Fd 4FeCN isotopologs, [57FeFe3S4]+ and [Fe57Fe3S4]+, show hyperfine coupling characteristic for [Fe4S4]+ clusters, particularly for the Fe to which cyanide binds. Thus, the low spin density on13C is not due to low spin density on the Fe ion to which it binds. Further theoretical work is needed to explain the contrast between the strong electronic effect of cyanide ion binding with the low spin density on the ligand. 相似文献
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Grosnick D Wright SC Bolton RD Cooper MD Frank JS Hallin AL Heusi PA Hoffman CM Hogan GE Mariam FG Matis HS Mischke RE Piilonen LE Sandberg VD Sanders GH Sennhauser U Werbeck R Williams RA Wilson SL Hofstadter R Hughes EB Ritter MW Highland VL McDonough J 《Physical review letters》1986,57(26):3241-3244
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