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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.
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
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
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
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
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
27 ng region of the nonmetallated Cu(A)-binding cupredoxin domain, arising from microsecond to second dy
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
36 r copper sites are present in the ubiquitous cupredoxin fold, able to bind one or two copper ions.
38 copper sites have been found to date within cupredoxin folds: blue type 1 (T1) copper, red type 2 (T
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
45 ne fVIIIa, whereas substitution of the first cupredoxin-like A1 subdomain resulted in a dissociation
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
50 mi there is no effect, and thus in these two cupredoxins loop contraction does not significantly infl
57 of the extremely stable and highly oxidizing cupredoxin rusticyanin from Thiobacillus ferrooxidans ha
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
70 des an active site environment in all of the cupredoxins which is preferable for Cu(II), whereas prev
72 tion potentials reported for any mononuclear cupredoxin, without perturbing the metal binding site be
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