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1 cant influence on the reduction potential of pseudoazurin.
2 ease nitrite reductase activity, but loss of pseudoazurin and cytochrome c(2) together reduced nitrit
4 ing effects on the pKa for the His ligand in pseudoazurin and plastocyanin due to subtle differences
6 ectroscopy studies in which cytochrome c550, pseudoazurin, and cytochrome c peroxidase were all prese
8 ediate populated during the refolding of apo-pseudoazurin appears to be obligate and on the folding p
11 of (1)H NMR spectroscopy, which showed that pseudoazurin binds closely enough to the electron-transf
13 of a single site, although results at higher pseudoazurin concentrations are complicated by the dimer
14 he native and two mutants (P80A and P80I) of pseudoazurin from Alcaligenes faecalis S-6 in oxidized a
15 16Phe variant and that of Met16 in wild type pseudoazurin identifies that this position provides an i
16 the chemical shift perturbation pattern for pseudoazurin in the presence of the peroxidase revealed
17 lanation for their different reactivities to pseudoazurin or azurin and supporting the view that elec
18 The paramagnetic (1)H NMR spectrum of Cu(II) pseudoazurin [PACu(II)] contains eight directly observed
19 the loop in the reduced proteins, and in the pseudoazurin (Paz) and plastocyanin (Pc) variants the va
20 e copper proteins (BCPs): amicyanin, azurin, pseudoazurin, plastocyanin, stellacyanin, and rusticyani
23 lecular docking simulation of the binding of pseudoazurin to the peroxidase in combination with the c
24 pression of paz, encoding the copper protein pseudoazurin, was highly reduced in the actR or fnrN mut
25 contact, stabilizing the coordinated form of pseudoazurin whereas in plastocyanin protonation and dis
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