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1 y due to the pKa values of cytochrome bH and Rieske iron sulfur protein.
2 ulated gene cluster including an alternative Rieske iron-sulfur protein.
3 the bc1 complex, where it interacts with the Rieske iron-sulfur protein.
5 tigmatellin with H-bonds between H161 of the Rieske iron-sulfur protein and E272 of the cyt b protein
6 ast to the loss of F(X), F(B), and F(A), the Rieske iron-sulfur protein and the non-heme iron in phot
8 be reduced in SMP via cytochrome c, and the Rieske iron-sulfur protein by ascorbate and faster by as
9 and Tyr-185 in the Saccharomyces cerevisiae Rieske iron-sulfur protein by site-directed mutagenesis
13 = 9 nm, raises the midpoint potential of the Rieske iron-sulfur protein from 285 to 385 mV, and shift
14 RNA interference of the complex III subunit Rieske iron sulfur protein in the cytochrome b-null cell
15 complex exists as a dimer with intertwining Rieske iron-sulfur proteins in solution, four Rhodobacte
17 The correlation between the import of the Rieske iron-sulfur protein into the mitochondrial matrix
20 sfer in vitro between soluble domains of the Rieske iron-sulfur protein (ISP) and cytochrome f subuni
22 stantial movement of the soluble head of the Rieske iron-sulfur protein (ISP) between reaction domain
24 essentiality of head domain movement of the Rieske iron-sulfur protein (ISP) during bc(1) catalysis,
25 ave provided evidence that a movement of the Rieske iron-sulfur protein (ISP) extrinsic domain is ess
26 he oriented cyt b(6)f complex shows that the Rieske iron-sulfur protein (ISP) is in distinct orientat
27 nt of the extramembrane (head) domain of the Rieske iron-sulfur protein (ISP) is involved in electron
28 implied that a large amplitude motion of the Rieske iron-sulfur protein (ISP) is required to mediate
29 nt of the extramembrane domain (head) of the Rieske iron-sulfur protein (ISP) may play an important r
30 osed that the soluble domain of the [2Fe-2S] Rieske iron-sulfur protein (ISP) must rotate by ca. 60 d
33 ) b6f and the cyt bc1 complexes incorporate 'Rieske' iron-sulfur protein (ISP) domain movements to ga
34 onstant was also not greatly affected by the Rieske iron-sulfur protein mutations Y156W, S154A, or S1
35 ted with a small interfering RNA against the Rieske iron-sulfur protein of mitochondrial complex III
36 between post-translational processing of the Rieske iron-sulfur protein of Saccharomyces cerevisiae a
37 NA carrying the Rip1 gene, which encodes the Rieske iron-sulfur protein of Schizosaccharomyces pombe,
38 ue COOH-terminal polypeptide fragment of the Rieske iron-sulfur protein of the cytochrome b6f complex
39 on of the excess purified head domain of the Rieske iron-sulfur protein partially restored the proton
40 aminosus complex and (ii) acetylation of the Rieske iron-sulfur protein (PetC) at the N terminus, a p
43 ion of these requirements with regard to the Rieske iron-sulfur protein QcrA of Bacillus subtilis.
44 bc(1) complex lacking the head domain of the Rieske iron-sulfur protein, removed by thermolysin diges
45 ffect when engineered into the budding yeast Rieske iron-sulfur protein Rip1, revealing remarkable co
47 plexes in mouse lung fibroblasts lacking the Rieske iron-sulfur protein (RISP knockout [KO]cells), on
48 ated by ablation of the genes coding for the Rieske iron-sulfur protein (RISP) and COX10, respectivel
49 ing Cre-mediated conditional deletion of the Rieske iron-sulfur protein (RISP) of Complex III was gen
50 aenorhabditis elegans isp-1 gene encodes the Rieske iron-sulfur protein subunit of cytochrome c oxido
54 ansfected with small interfering RNA against Rieske iron sulfur protein, the hypoxia-mediated Na,K-AT
55 rogen bond to the iron-sulfur cluster of the Rieske iron-sulfur protein to a cysteine results in a re
57 ing a small hairpin RNA directed against the Rieske iron-sulfur protein, we show that site III of the
58 ex indicate that the catalytic domain of the Rieske iron-sulfur protein, which carries the [2Fe-2S] c
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