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1 ein Cu(A) center to-date has used a modified cupredoxin.
2 tegies that have proven successful in native cupredoxins.
3 tuning spectroscopic and redox properties of cupredoxins.
4 member of a family of metalloproteins called cupredoxins.
5 a par with the blue copper proteins known as cupredoxins.
6 e plantacyanins, uclacyanins, and most other cupredoxins.
7 observed in other structurally characterized cupredoxins.
8 V vs SHE) is much lower than those for known cupredoxins.
9 als an unprecedented trimer of single domain cupredoxins.
10  and more intersheet connectivity than other cupredoxins.
11 ing methylamine dehydrogenase (MADH) and the cupredoxin amicyanin.
12 l of 680 mV, roughly twice that of any other cupredoxin, and it is optimally active at pH values < or
13 ligand tuning of spectroscopic properties in cupredoxins, and demonstrate the power of using unnatura
14                                              Cupredoxins are electron-transfer proteins that have act
15 blue, which are found in organisms where the cupredoxins are pseudoazurins and azurins, respectively.
16 erlying mechanism of the action of bacterial cupredoxin azurin in the regression of breast cancer and
17 ble of tuning the reduction potential of the cupredoxin azurin over a 700 mV range, surpassing the hi
18 cofactor of AADH to the type I copper of the cupredoxin azurin.
19 l intermediate that has not been reported in cupredoxins before, with intense electronic absorption m
20  water), a trimeric protein structure, and a cupredoxin beta-barrel fold have been established by X-r
21 mi) has been introduced into three different cupredoxin beta-barrel scaffolds.
22 s a number of similarities to those of other cupredoxins, but differences are found concerning the Cu
23  rusticyanin may also be enhanced over other cupredoxins by a more extensive internal hydrogen bondin
24       These results suggest that mononuclear cupredoxins can have a wide range of structural features
25 ations based on BiGGER is employed on MSP119-cupredoxin complexes.
26 rength axial ligand has been demonstrated in cupredoxins, converting the blue copper center to a red
27 vides an underlying link between the various cupredoxin copper sites and possible experimental eviden
28           Moreover, the native rusticyanin's cupredoxin core and the type 1 Cu site closely resemble
29 perties of unique electron-transfer sites in cupredoxins (CuHis(2) Cys) or rubredoxins (FeCys(4) ).
30 binuclear Cu(A) center, an electron transfer cupredoxin domain of photosynthetic and respiratory comp
31                           The copper-binding cupredoxin domain was observed in both Gephyrocapsa spec
32 ng region of the nonmetallated Cu(A)-binding cupredoxin domain, arising from microsecond to second dy
33  trimer, of which each subunit comprises two cupredoxin domains.
34 es between the two quinoproteins and the two cupredoxins, each is specific for its respective partner
35 ue structural feature of this protein in the cupredoxin family and has been speculated to be responsi
36                      Azurin, a member of the cupredoxin family of copper containing redox proteins, p
37  binding site beyond what is typical for the cupredoxin family of proteins.
38 or apo-rusticyanin and other proteins of the cupredoxin family.
39 l electron-transfer protein belonging to the cupredoxin family.
40                                          The cupredoxin fold is an important motif in numerous protei
41 r copper sites are present in the ubiquitous cupredoxin fold, able to bind one or two copper ions.
42 novo scaffold, especially one removed from a cupredoxin fold, remained.
43 first example of a type 2 copper center in a cupredoxin fold.
44 e and function disconnected from the overall cupredoxin fold.
45 ven difficult to recapitulate outside native cupredoxin folds.
46  copper sites have been found to date within cupredoxin folds: blue type 1 (T1) copper, red type 2 (T
47 emotherapeutic application of this bacterial cupredoxin for the treatment of breast cancer.
48 lative to the unique Cu-S characteristics of cupredoxins, from which it is concluded that Sco does no
49  type 2 red copper (T2 Cu), and purple Cu(A) cupredoxins have been proposed, but the structural featu
50 reductases, electron donation from a reduced cupredoxin is an essential step in the reduction of nitr
51                             Here we report a cupredoxin isolated from the nitrifying archaeon Nitroso
52     Subsequently, substitution of the second cupredoxin-like A1 subdomain resulted in a dissociation
53 ne fVIIIa, whereas substitution of the first cupredoxin-like A1 subdomain resulted in a dissociation
54                              We propose that cupredoxin-like A1 subdomains in fVIII contain inter-spe
55  a multicopper oxidase (MCO) that contains 3 cupredoxin-like beta-barrel domains and 4 copper ions lo
56 te that the FG helix of the COOH-terminal A1 cupredoxin-like subdomain of fVIII may be under selectiv
57 he three fVIII A domains each consist of two cupredoxin-like subdomains.
58 mi there is no effect, and thus in these two cupredoxins loop contraction does not significantly infl
59 e positions and scaffolds, refinement of our cupredoxin models, and enhancement of nitrite reductase
60                   EfeO is periplasmic with a cupredoxin N-terminal domain; EfeB is also periplasmic a
61 reductases, one green and two blue, and five cupredoxins, one pseudoazurin and four azurins.
62 ve an electron from redox partner proteins a cupredoxin or a c-type cytochrome.
63  is now predictable across the full range of cupredoxin potentials.
64                                  Mononuclear cupredoxin proteins usually contain a coordinately satur
65 or the evolutionary relationship between the cupredoxin proteins.
66 of the extremely stable and highly oxidizing cupredoxin rusticyanin from Thiobacillus ferrooxidans ha
67                                   Like other cupredoxins, rusticyanin is a copper-containing metallop
68 indings also lend physiological relevance to cupredoxin site biosynthesis.
69  regarding the evolutionary link between all cupredoxin sites as well as the in vivo assembly of Cu(A
70 ins of differences in redox potentials among cupredoxins (small blue type I copper-containing protein
71 l of the interface between the core trimeric cupredoxin structure of CuNiR and the tethered cytochrom
72 ignificantly homologous with the mononuclear cupredoxins such as plastocyanin, azurin, or rusticyanin
73         Members of the ENOD subfamily of the cupredoxin superfamily do not appear to bind copper and
74                                    Among the cupredoxins tested, rusticyanin forms a well defined com
75       The phytocyanins are a family of plant cupredoxins that have been subdivided into the stellacya
76         Furthermore, we identified conserved cupredoxins, thaumatin-like proteins and lytic polysacch
77                              Also like other cupredoxins, the copper ion is coordinated by a cluster
78                     By comparison with other cupredoxins, the three-dimensional structure of rusticya
79                   The type 1 copper sites of cupredoxins typically have a His(2)Cys equatorial ligand
80 des an active site environment in all of the cupredoxins which is preferable for Cu(II), whereas prev
81             Given the structural homology of cupredoxins with the Fab domain of monoclonal antibodies
82 tion potentials reported for any mononuclear cupredoxin, without perturbing the metal binding site be