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1 est activation energy was oxidation of bound ubihydroquinone.
2 rane proteins that catalyze the oxidation of ubihydroquinone and the reduction of cytochrome c in mit
3 e-substrate complex required two substrates, ubihydroquinone binding from the lipid phase and the ext
4                                          The ubihydroquinone-cytochrome c oxidoreductase (or the cyto
5 eriments using mutants of the bc(1) complex (ubihydroquinone-cytochrome c oxidoreductase) iron-sulfur
6                                              Ubihydroquinone:cytochrome (cyt) c oxidoreductase (bc1 c
7 tosynthetic electron transfer protein called ubihydroquinone:cytochrome (cyt) c oxidoreductase or cyt
8                                          The ubihydroquinone:cytochrome (cyt) c oxidoreductase, or bc
9           The cytochrome c(1) subunit of the ubihydroquinone:cytochrome c oxidoreductase (bc(1) compl
10                         Native structures of ubihydroquinone:cytochrome c oxidoreductase (bc(1) compl
11                  Structures of mitochondrial ubihydroquinone:cytochrome c oxidoreductase (bc(1) compl
12 allographic structures for the mitochondrial ubihydroquinone:cytochrome c oxidoreductase (bc(1) compl
13          The cytochrome (cyt) c1 heme of the ubihydroquinone:cytochrome c oxidoreductase (bc1 complex
14                                          The ubihydroquinone:cytochrome c oxidoreductase (cyt bc(1))
15 none (SQ) at the Qi-site of the bc1 complex (ubihydroquinone:cytochrome c oxidoreductase (EC 1.10.2.2
16                                          The ubihydroquinone:cytochrome c oxidoreductase, or bc(1) co
17            DPA is specific to the QO site of ubihydroquinone:cytochrome c oxidoreductase, where it in
18 ) complex is the stoichiometry of ubiquinone/ubihydroquinone occupancy.
19   The cleavage was affected significantly by ubihydroquinone oxidation (Q(o)) and ubiquinone reductio
20 The bc(1) complex has two catalytic domains, ubihydroquinone oxidation (Q(o)) and ubiquinone reductio
21 e [2Fe-2S] cluster with the occupants of the ubihydroquinone oxidation (Q(o)) catalytic site.
22           Cyt cy, despite its rereduction by ubihydroquinone oxidation in the millisecond time range,
23 r subunit [2Fe-2S] cluster domain during the ubihydroquinone oxidation reaction catalyzed by the cyto
24             The pH dependence of the rate of ubihydroquinone oxidation reflected the pK on the oxidiz
25  of the enzyme but not for a single turnover ubihydroquinone oxidation site catalysis.
26 ng which the [2Fe-2S] cluster interacts with ubihydroquinone oxidation site occupants and catalyzes u
27 ge by enhancing superoxide production at the ubihydroquinone oxidation site.
28                    The activation energy for ubihydroquinone oxidation was independent of the concent
29 inone oxidation site occupants and catalyzes ubihydroquinone oxidation, and a "macro-movement," durin
30 suggesting that this subunit may move during ubihydroquinone oxidation.
31 domain as a device to shuttle electrons from ubihydroquinone to cyt c(1) (or cyt f).
32 or electron transfer from cytochrome b-bound ubihydroquinone to cytochrome c1 of the cytochrome bc1 c
33 purified b-c1 subcomplex had a nonfunctional ubihydroquinone (UQH2) oxidation (Qo) site, but it conta

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