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

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