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PDBsum entry 1r1c
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protein ligands metals Protein-protein interface(s) links
Electron transport PDB id
1r1c

 

 

 

 

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Contents
Protein chains
128 a.a. *
Ligands
REP ×4
Metals
CU1 ×4
Waters ×303
* Residue conservation analysis
PDB id:
1r1c
Name: Electron transport
Title: Pseudomonas aeruginosa w48f/y72f/h83q/y108w-azurin re(phen)(co) 3(his107)
Structure: Azurin. Chain: a, b, c, d. Engineered: yes. Mutation: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Gene: azu or pa4922. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.90Å     R-factor:   0.224     R-free:   0.260
Authors: J.E.Miller,C.Gradinaru,B.R.Crane,A.J.Di Bilio
Key ref: J.E.Miller et al. (2003). Spectroscopy and reactivity of a photogenerated tryptophan radical in a structurally defined protein environment. J Am Chem Soc, 125, 14220-14221. PubMed id: 14624538 DOI: 10.1021/ja037203i
Date:
23-Sep-03     Release date:   30-Sep-03    
PROCHECK
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 Headers
 References

Protein chains
P00282  (AZUR_PSEAE) -  Azurin from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Seq:
Struc: 		148 a.a.
128 a.a.*
Key:    Secondary structure  CATH domain
* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 

 
DOI no: 10.1021/ja037203i J Am Chem Soc 125:14220-14221 (2003)
PubMed id: 14624538  
 
 
Spectroscopy and reactivity of a photogenerated tryptophan radical in a structurally defined protein environment.
J.E.Miller, C.Grădinaru, B.R.Crane, A.J.Di Bilio, W.A.Wehbi, S.Un, J.R.Winkler, H.B.Gray.
 
  ABSTRACT  
 
Near-UV irradiation of structurally characterized [Re(I)(CO)3(1,10-phenanthroline)(Q107H)](W48F/Y72F/H83Q/Y108W)AzM(II) [Az = Pseudomonas aeruginosa azurin, M = Cu, Zn]/[Co(NH3)5Cl]Cl2 produces a tryptophan radical (W108*) with unprecedented kinetic stability. After rapid formation (k = 2.8 x 106 s-1), the radical persists for more than 5 h at room temperature in the folded ReAzM(II) structure. The absorption spectrum of ReAz(W108*)M(II) exhibits maxima at 512 and 536 nm. Oxidation of K4[Mo(CN)8] by ReAz(W108*)Zn(II) places the W108*/W108 reduction potential in the protein above 0.8 V vs NHE.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21469225 A.M.Blanco-Rodríguez, A.J.Di Bilio, C.Shih, A.K.Museth, I.P.Clark, M.Towrie, A.Cannizzo, J.Sudhamsu, B.R.Crane, J.Sýkora, J.R.Winkler, H.B.Gray, S.Záliš, and A.Vlček (2011).
Phototriggering electron flow through Re(I)-modified Pseudomonas aeruginosa azurins.
  Chemistry, 17, 5350-5361.  
21301713 C.Bernini, R.Pogni, F.J.Ruiz-Dueñas, A.T.Martínez, R.Basosi, and A.Sinicropi (2011).
EPR parameters of amino acid radicals in P. eryngii versatile peroxidase and its W164Y variant computed at the QM/MM level.
  Phys Chem Chem Phys, 13, 5078-5098.  
21331408 C.M.Yang (2011).
Biometal binding-site mimicry with modular, hetero-bifunctionally modified architecture encompassing a Trp/His motif: insights into spatiotemporal noncovalent interactions from a comparative spectroscopic study.
  Dalton Trans, 40, 3008-3027.  
20669189 C.M.Yang, and J.Zhang (2010).
Insights into intramolecular Trp and His side-chain orientation and stereospecific π interactions surrounding metal centers: an investigation using protein metal-site mimicry in solution.
  Chemistry, 16, 10854-10865.  
20830385 J.A.Gregersen, and F.Tureček (2010).
Mass-spectrometric and computational study of tryptophan radicals (Trp + H)˙ produced by collisional electron transfer to protonated tryptophan in the gas phase.
  Phys Chem Chem Phys, 12, 13434-13447.  
19805263 A.T.Smith, W.A.Doyle, P.Dorlet, and A.Ivancich (2009).
Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase.
  Proc Natl Acad Sci U S A, 106, 16084-16089.  
19159240 S.Stoll, A.Gunn, M.Brynda, W.Sughrue, A.C.Kohler, A.Ozarowski, A.J.Fisher, J.C.Lagarias, and R.D.Britt (2009).
Structure of the biliverdin radical intermediate in phycocyanobilin:ferredoxin oxidoreductase identified by high-field EPR and DFT.
  J Am Chem Soc, 131, 1986-1995.  
18433127 H.D.Connor, B.E.Sturgeon, C.Mottley, H.J.Sipe, and R.P.Mason (2008).
L-tryptophan radical cation electron spin resonance studies: connecting solution-derived hyperfine coupling constants with protein spectral interpretations.
  J Am Chem Soc, 130, 6381-6387.  
16443605 R.Pogni, M.C.Baratto, C.Teutloff, S.Giansanti, F.J.Ruiz-Dueñas, T.Choinowski, K.Piontek, A.T.Martínez, F.Lendzian, and R.Basosi (2006).
A tryptophan neutral radical in the oxidized state of versatile peroxidase from Pleurotus eryngii: a combined multifrequency EPR and density functional theory study.
  J Biol Chem, 281, 9517-9526.  
16983713 Z.Bao, S.Sun, J.Li, X.Chen, S.Dong, and H.Ma (2006).
Direct identification of tryptophan in a mixture of amino acids by the naked eye.
  Angew Chem Int Ed Engl, 45, 6723-6725.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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