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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
5 eriments using mutants of the bc(1) complex (ubihydroquinone-cytochrome c oxidoreductase) iron-sulfur
7 tosynthetic electron transfer protein called ubihydroquinone:cytochrome (cyt) c oxidoreductase or cyt
12 allographic structures for the mitochondrial ubihydroquinone:cytochrome c oxidoreductase (bc(1) compl
15 none (SQ) at the Qi-site of the bc1 complex (ubihydroquinone:cytochrome c oxidoreductase (EC 1.10.2.2
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
23 r subunit [2Fe-2S] cluster domain during the ubihydroquinone oxidation reaction catalyzed by the cyto
26 ng which the [2Fe-2S] cluster interacts with ubihydroquinone oxidation site occupants and catalyzes u
29 inone oxidation site occupants and catalyzes ubihydroquinone oxidation, and a "macro-movement," durin
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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