Azurin Pseudomonas aeruginosa

Antholine, W.E., Hanna, P.M., and McMillan, D.R. 1993. Low frequency EPR of Pseudomonas aeruginosa azurin analysis of ligand superhyperfine structure from a type 1 copper site. Biophysical Journal 64 267-272. 

K. K. Turoverov, I. M. Kuznetsova, and V. N. Zaitsev, The environment of the tryptophan residue in Pseudomonas aeruginosa azurin and its fluorescence properties, Biophys. Chem. 23, 79-89 (1985). 

Fig. 5. View of the blue copper and a5Ru(His83) centers in ruthenated Pseudomonas aeruginosa azurin [28]...

Intramolecular Ru(II) to Cu(II) ET rates have been measured in two other blue copper proteins, stellacyanin [42, 43] and azurin [9, 13, 28]. Pseudomonas aeruginosa azurin has been ruthenated at His83 [13] (Fig. 5). The intramolecular Ru(II) to Cu(II) ET rate of 1.9 s was found to be independent of temperature [28]. The Cu reorganization enthalpy was estimated to be < 7 kcal/mol [13, 28], a value confirming that blue copper is structured for efficient ET. Again, a blue copper ET rate is low in comparison with heme protein rates over similar distances (at similar driving forces) (Table 1). 

Groeneveld etal. (1986) from an EXAFS study of Pseudomonas aeruginosa azurin, in which, on reduction, indications for a significantly shorter Cu-S bond were observed. 

A qualitative understanding of these features was provided in 1978 when the crystal structure of poplar leaf plastocyanin and Pseudomonas aeruginosa azurin appear-ed 2,73) proteins appears to be coordinated by two histidines with... 

Rhenium carbonyl complexes were used as probes in biological systems. Photoexcitation of [Re(phen)(CO)3(H83)]+AzM2+ and [Re(phen)(CO)3(H107)] + AzM2+ (Az = Pseudomonas aeruginosa azurin M = Cu or Zn) in the presence of the oxidative quencher, Co(NH3)5C1, resulted in the formation... 

IN SITU AND AFM OF SINGLE-METAL METALLOPROTEINS HORSE HEART CYTOCHROME C AND PSEUDOMONAS AERUGINOSA AZURIN... 

Fig. 17 Photoinduced electron transfer in Re-derivatized Pseudomonas aeruginosa azurin (Az) by hopping through a proximal tryptophan Re,(CO)3(Me2-phen)(H124)l(W122)IAzCu. Only the part of the protein structure that bears the Re chromophore (at the left end of the chain) is shown. The trp indole group is nearly parallel with the phen ligand, sticking up from the chain. The Cu center is on the right. Reprinted with permission from [43]...

Fig.3. 800-MHz NMR spectra of oxidized (A) Pseudomonas aeruginosa azurin, (B) spinach plastocyanin, and (C) cucumber stellacyanin recorded in D2O solution. The letters identify the resonance of the equivalent proton in the three proteins. In the insets the far-downheld regions containing signals not observable in direct detection are shown (Bertini et al., 2000). The positions and the linewidths of the signals of the oxidized species were obtained using saturation transfer experiments over the far-downheld region by measuring the intensity of the exchange connectivity with the corresponding signal in the reduced species (Bertini et al., 1999, 2000).

Fig.4. NMR spectra of cobalt(II)-substituted (A) Pseudomonas aeruginosa azurin (Moratal Mascarell a/., 1993b) ( ) Achromohacter cycloclastes pseudoazurin (Fernandez et al., submitted for publication), and (C) Rhus vernacifera stellacyanin (Vila, 1994). Spectra (A) and (C) were recorded at 200 MHz at 313 K, whereas spectrum (B) was recorded at 600 MHz and 318 K. All the samples were in 50 mM phosphate buffer at pH 6 in water solution.

The wtp5 and wtp9 recombinant wild-type structures are from Pseudomonas aeruginosa azurin at pH 5.5 and 9.0. The data are from Nar et al. (96). 

Fig. 5. Stereo plot of the overlay of the type-1 copper sites for poplar plastocyanin (thin line), Pseudomonas aeruginosa azurin (medium line), and ascorbate oxidase (thick line).

Ralle M, Berry SM, Nilges Ml, Gieselman MD, Van der Donk WA, Lu Y, Blackburn NJ. The selenocysteine-substituted blue copper center spectroscopic investigations of Cysl 12SeCys pseudomonas aeruginosa azurin. J. Am Chem. Soc. 2004 126 7244— 7256. 

Garner DK, Vaughan MD, Hwang HI, Savelieff MG, Berry SM, Honek JE, Lu Y. Reduction potential tuning of the blue copper center in pseudomonas aeruginosa azurin by the axial methionine as probed by unnatural amino acids. J. Am. Chem. Soc. 2006 128 15608-15617. 

Figure 2. Ribbon structure representation of the crystal structure of Ru(bpy)2(im)(His83) -labeled Pseudomonas aeruginosa azurin [26].

Fig 6. A comparison of UV-VIS absorption spectra for the Cu(II) forms of Pseudomonas aeruginosa azurin (—) and spinach plastocyanin (—). 

Fig, 9. Variation of reduction potential with pH for the Pseudomonas aeruginosa azurin ACu(II)/ACu(I) couple from titrations with [FelCNlel ( ), and from rate constants for ACu(I) + [FelCNleP" and [FelCNle) " + ACu(II) ( ). 

Nar, H., Messerschmidt, A., Huber, R., et al. (1991) Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. ApH-induced conformational transition involves a peptide bond flip. J. Mol. Biol., 221(3), 765-772. 

G. W., Andersen, J.E.T., and Ulstrup, J. (2000) Molecular monolayers and interfadal electron transfer of Pseudomonas aeruginosa azurin on Au(l 11). Journal of the American Chemical Society, 122, 4047-4055. 

Jensen, P.S., Chi, Q., Zhang, J., and Ulstrup, J. (2009) Long-range interfadal electrochemical electron transfer of Pseudomonas aeruginosa azurin-gold nanoparticle hybrid systems. Journal of Physical Chemistry C, 113,13993-14000. 

A model of the structure of the blue single copper centre metalloprotein Pseudomonas aeruginosa azurin, is shown in Fig. 7-16. 

Vanpouderoyen G, Mazumdar S, Hunt NI, Hill HAO, Canters GW (1994) The introduction of a negative charge into the hydrophobic patch of Pseudomonas aeruginosa azurin affects the alectron self-exchange rate and the electrochemistry. Eur J Biochem 222 583-588... 

Mizoguchi TJ, Dibilio AJ, Gray HB, Richards JH (1992) Blue to type-2 binding - copper(II) and cobalt(II) derivatives of a Cysl 12Asp Mutant of Pseudomonas aeruginosa azurin. J Am Chem Soc 114 10076-10078... 

Lancaster KM, Y okoyama K, Richards JH, Winkler JR, Gray FIB (2009) High-potential C112D/ M121X (X = M, E H, L) Pseudomonas aeruginosa azurins. Inorg Chem 48 1278-1280... 

Lancaster KM, Sproules S, Palmer JH, Richards JH, Gray HB (2010) Outer-sphere effects on reduction potentials of copper sites in proteins the curious case of high potential type 2 C112D/M121E Pseudomonas aeruginosa azurin. J Am Chem Soc 132 14590-14595... 

Lancaster KM, Farver O, Wherland S, Crane EJ, Richards JH, Pecht I, Gray HB (2011) Electron transfer reactivity of type zero Pseudomonas aeruginosa azurin. J Am Chem Soc 133 4865 1873... 

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