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1 rsulfide dioxygenase (ETHE1), rhodanese, and sulfite oxidase.
2 ubstrate binding and oxidation of sulfite by sulfite oxidase.
3 is remarkably similar to the low-pH form of sulfite oxidase.
4 he proposed structure of the high-pH form of sulfite oxidase.
5 nd capable of donating bound MPT to MPT-free sulfite oxidase.
6 concomitantly with the insertion of MPT into sulfite oxidase.
7 proteins: cytochrome c, adenylate kinase and sulfite oxidase.
8 calculations are extended to oxo transfer by sulfite oxidase.
9 mutation was also generated in cloned human sulfite oxidase.
10 t, 9 closely resembles the oxidized sites in sulfite oxidase and assimilatory nitrate reductase as de
11 ing partial misfolding and monomerization of sulfite oxidase and attenuating both substrate binding a
12 persulfide dioxygenase (PDO), rhodanese, and sulfite oxidase and converts H2S to thiosulfate and sulf
14 ed the characteristic absorption spectrum of sulfite oxidase and exhibited steady state and rapid kin
15 of the isolated molybdenum domains of native sulfite oxidase and of the R160Q mutant showed significa
16 are sufficient for the insertion of MPT into sulfite oxidase and the conversion of MPT into Moco in t
17 s in crystallizing recombinant human and rat sulfite oxidases and the failure to clone the chicken su
19 sulfite oxidase, Arabidopsis thaliana plant sulfite oxidase, and the bacterial sulfite dehydrogenase
21 remarkably similar to that found in chicken sulfite oxidase, Arabidopsis thaliana plant sulfite oxid
25 onance Raman spectra of oxidized A. thaliana sulfite oxidase catalytically cycled in both H2(16)O and
31 in the sulfite oxidase gene responsible for sulfite oxidase deficiency in a 5-year-old girl was iden
34 tations identified in patients with isolated sulfite oxidase deficiency, the G473D variant is of part
35 for confirmatory testing of cystic fibrosis, sulfite oxidase deficiency, urolithiasis, and other diso
36 crystal structures of the wild type and the sulfite oxidase deficiency-causing R138Q (R160Q in human
37 The active sites of the xanthine oxidase and sulfite oxidase enzyme families contain one pterin-dithi
51 nter of the pathogenic R160Q mutant of human sulfite oxidase (hSO) confirms the presence of three dis
52 dies on the pathogenic R160Q mutant of human sulfite oxidase (HSO) have shown that Mo-heme intramolec
55 0Q in humans) variant of recombinant chicken sulfite oxidase in the resting and sulfate-bound forms.
56 ble to reconstitute molybdopterin (MPT)-free sulfite oxidase in vitro with the molybdenum cofactor (M
60 e reductive half-reaction of wild-type human sulfite oxidase, k(red)(heme) changed very little over t
61 he first time in rapid reaction assays using sulfite oxidase lacking the N-terminal heme-containing d
62 subsequent reconstitution of MoCo-free human sulfite oxidase-molybdenum domain yielding a fully activ
64 te forms of the molybdenum-containing enzyme sulfite oxidase possess a b-type cytochrome prosthetic g
67 f this residue in the catalytic mechanism of sulfite oxidase, serine and alanine variants at position
69 d low pH (lpH) forms of native chicken liver sulfite oxidase (SO) and recombinant human SO have been
70 Protein film voltammetry of chicken liver sulfite oxidase (SO) bound at the pyrolytic graphite "ed
72 8D were identified in patients with isolated sulfite oxidase (SO) deficiency, and the equivalent amin
79 sulfate reductase and the sulfite scavengers sulfite oxidase (SO), sulfite reductase, UDP-sulfoquinov
81 f this residue in the catalytic mechanism of sulfite oxidase, steady-state and stopped-flow analyses
83 o either the xanthine dehydrogenase (XDH) or sulfite oxidase (SUOX) families, and these have pyranopt
85 to emanate from my laboratory have been the sulfite oxidase, the several superoxide dismutases, the
90 In this study, we have investigated IET in sulfite oxidase using laser flash photolysis as a functi
91 heme and molybdenum centers of chicken liver sulfite oxidase varies from approximately 20 to 1400 s(-
93 ybdate in the reconstitution mixture, active sulfite oxidase was obtained, revealing that in vitro MP
95 ther bovine serum albumin or Moco-containing sulfite oxidase was used in place of aposulfite oxidase.
96 ase, the residue Tyr(322) (Tyr(343) in human sulfite oxidase) was found to directly interact with a b
97 the role of conformational changes on IET in sulfite oxidase, which helps to clarify the inconsistenc
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