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1 ase), or by Escherichia coli cysJI (encoding sulfite reductase).
2 e and of dsrC, associated with dissimilatory sulfite reductase).
3 cation is unique and independent of CysI and sulfite reductase.
4 first report of a coenzyme F(420)-dependent sulfite reductase.
6 n suggest that DCP68 is the siroheme protein sulfite reductase, a ferredoxin-dependent enzyme that pa
10 -terminal half a dissimilatory-type siroheme sulfite reductase, and Fsr catalyzes the corresponding p
11 oad similarity to the hemoprotein subunit of sulfite reductase but has many significant differences i
13 flavin oxidoreductase component of the CysJI sulfite reductase complex (CysJ(8)I(4)), we show that th
14 mparative sequence analysis of dissimilatory sulfite reductase (DSR) genes from closely and distantly
15 lic processes, and profiles of dissimilatory sulfite reductase (dsr) transcripts are consistent with
16 CR targeting the 16S rRNA, dissimilatory (bi)sulfite reductase (dsrAB), and dissimilatory arsenate re
19 The initial rate parameters for the purified sulfite reductase from M. tuberculosis were determined u
20 el, highly active, coenzyme F(420)-dependent sulfite reductase (Fsr) with a cell extract specific act
21 t may interact with HdrABC and dissimilatory sulfite reductase gamma subunit (DsrC) to perform novel
22 hic patterns of the functional dissimilatory sulfite reductase gene (dsrA) and the 16S rRNA gene in s
23 ologue of the gamma subunit of dissimilatory sulfite reductase, has been determined by NMR spectrosco
25 The active center of the Escherichia coli sulfite reductase hemoprotein (SiRHP) is exquisitely des
26 nd nitrite catalyzed by the Escherichia coli sulfite reductase hemoprotein (SiRHP), we have determine
27 s coding for DsrAB, the enzyme dissimilatory sulfite reductase, inevitably also contain the gene codi
29 e, the prosthetic group for both nitrite and sulfite reductases, is a methylated, iron-containing mod
34 Like their nitrite reductase counterparts, sulfite reductases require a siroheme cofactor for catal
40 ences or could arise from alterations of the sulfite reductase structure that arise from the isolatio
41 dentification of virus-encoded dissimilatory sulfite reductase suggests SUP05 viruses reprogram their
42 the sulfite scavengers sulfite oxidase (SO), sulfite reductase, UDP-sulfoquinovose synthase, and beta
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