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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
3 reen and two blue, and five cupredoxins, one pseudoazurin and four azurins.
4 ing effects on the pKa for the His ligand in pseudoazurin and plastocyanin due to subtle differences
5 found in organisms where the cupredoxins are pseudoazurins and azurins, respectively.
6 ectroscopy studies in which cytochrome c550, pseudoazurin, and cytochrome c peroxidase were all prese
7                    The Met16Phe and Met16Trp pseudoazurin, and Leu12Phe spinach and Leu14Phe Phormidi
8 ediate populated during the refolding of apo-pseudoazurin appears to be obligate and on the folding p
9         We conclude that cytochrome c550 and pseudoazurin bind at the same site on the cytochrome c p
10                                              Pseudoazurin binds at a single site on cytochrome c pero
11  of (1)H NMR spectroscopy, which showed that pseudoazurin binds closely enough to the electron-transf
12                           Our data show that pseudoazurin can readily donate electrons to both blue a
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
21                       The fit shows that apo-pseudoazurin rapidly forms a compact species that is sta
22                                paz encodes a pseudoazurin that is a donor of electrons to nitrite red
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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