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PDBsum entry 1jzf
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protein ligands metals links
Electron transport PDB id
1jzf

 

 

 

 

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Contents
Protein chain
128 a.a. *
Ligands
RTB
IME
Metals
_CU
Waters ×174
* Residue conservation analysis
PDB id:
1jzf
Name: Electron transport
Title: Pseudomonas aeruginosa oxidized azurin(cu2+) ru(tpy)(phen)(his83)
Structure: Azurin. Chain: a. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.50Å     R-factor:   0.218     R-free:   0.220
Authors: B.R.Crane,A.J.Di Bilio,J.R.Winkler,H.B.Gray
Key ref: B.R.Crane et al. (2001). Electron tunneling in single crystals of Pseudomonas aeruginosa azurins. J Am Chem Soc, 123, 11623-11631. PubMed id: 11716717 DOI: 10.1021/ja0115870
Date:
16-Sep-01     Release date:   17-Oct-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
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:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1021/ja0115870 J Am Chem Soc 123:11623-11631 (2001)
PubMed id: 11716717  
 
 
Electron tunneling in single crystals of Pseudomonas aeruginosa azurins.
B.R.Crane, A.J.Di Bilio, J.R.Winkler, H.B.Gray.
 
  ABSTRACT  
 
Rates of reduction of Os(III), Ru(III), and Re(I) by Cu(I) in His83-modified Pseudomonas aeruginosa azurins (M-Cu distance approximately 17 A) have been measured in single crystals, where protein conformation and surface solvation are precisely defined by high-resolution X-ray structure determinations: 1.7(8) x 10(6) s(-1) (298 K), 1.8(8) x 10(6) s(-1) (140 K), [Ru(bpy)2(im)(3+)-]; 3.0(15) x 10(6) s(-1) (298 K), [Ru(tpy)(bpy)(3+)-]; 3.0(15) x 10(6) s(-1) (298 K), [Ru(tpy)(phen)(3+)-]; 9.0(50) x 10(2) s(-1) (298 K), [Os(bpy)2(im)(3+)-]; 4.4(20) x 10(6) s(-1) (298 K), [Re(CO)3(phen)(+)] (bpy = 2,2'-bipyridine; im = imidazole; tpy = 2,2':6',2' '-terpyridine; phen = 1,10-phenanthroline). The time constants for electron tunneling in crystals are roughly the same as those measured in solution, indicating very similar protein structures in the two states. High-resolution structures of the oxidized (1.5 A) and reduced (1.4 A) states of Ru(II)(tpy)(phen)(His83)Az establish that very small changes in copper coordination accompany reduction but reveal a shorter axial interaction between copper and the Gly45 peptide carbonyl oxygen [2.6 A for Cu(II)] than had been recognized previously. Although Ru(bpy)2(im)(His83)Az is less solvated in the crystal, the reorganization energy for Cu(I) --> Ru(III) electron transfer falls in the range (0.6-0.8 eV) determined experimentally for the reaction in solution. Our work suggests that outer-sphere protein reorganization is the dominant activation component required for electron tunneling.
 

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.  
20683517 A.V.Kartashov, G.Serafini, M.Dong, S.Shipovskov, I.Gazaryan, F.Besenbacher, and E.E.Ferapontova (2010).
Long-range electron transfer in recombinant peroxidases anisotropically orientated on gold electrodes.
  Phys Chem Chem Phys, 12, 10098-10107.  
20945309 C.C.Ko, L.T.Lo, C.O.Ng, and S.M.Yiu (2010).
Photochemical synthesis of intensely luminescent isocyano rhenium(I) complexes with readily tunable structural features.
  Chemistry, 16, 13773-13782.  
19701722 M.B.Rajasekaran, S.Nilapwar, S.C.Andrews, and K.A.Watson (2010).
EfeO-cupredoxins: major new members of the cupredoxin superfamily with roles in bacterial iron transport.
  Biometals, 23, 1.  
19894966 A.M.Kuznetsov, I.G.Medvedev, and J.Ulstrup (2009).
Coulomb repulsion effect in two-electron nonadiabatic tunneling through a one-level redox molecule.
  J Chem Phys, 131, 164703.  
19746904 A.S.Lipton, R.W.Heck, W.A.de Jong, A.R.Gao, X.Wu, A.Roehrich, G.S.Harbison, and P.D.Ellis (2009).
Low temperature 65Cu NMR spectroscopy of the Cu+ site in azurin.
  J Am Chem Soc, 131, 13992-13999.  
20161522 H.B.Gray, and J.R.Winkler (2009).
Electron Flow through Proteins.
  Chem Phys Lett, 483, 1-9.  
19299503 K.Sato, C.Li, I.Salard, A.J.Thompson, M.J.Banfield, and C.Dennison (2009).
Metal-binding loop length and not sequence dictates structure.
  Proc Natl Acad Sci U S A, 106, 5616-5621.
PDB codes: 3fs9 3fsa 3fsv 3fsw 3fsz 3ft0
19190939 M.Lee, M.C.del Rosario, H.H.Harris, R.E.Blankenship, J.M.Guss, and H.C.Freeman (2009).
The crystal structure of auracyanin A at 1.85 A resolution: the structures and functions of auracyanins A and B, two almost identical "blue" copper proteins, in the photosynthetic bacterium Chloroflexus aurantiacus.
  J Biol Inorg Chem, 14, 329-345.  
19344235 S.Y.Reece, and D.G.Nocera (2009).
Proton-coupled electron transfer in biology: results from synergistic studies in natural and model systems.
  Annu Rev Biochem, 78, 673-699.  
18250895 C.Dennison (2008).
The role of ligand-containing loops at copper sites in proteins.
  Nat Prod Rep, 25, 15-24.  
18583608 C.Shih, A.K.Museth, M.Abrahamsson, A.M.Blanco-Rodriguez, A.J.Di Bilio, J.Sudhamsu, B.R.Crane, K.L.Ronayne, M.Towrie, A.Vlcek, J.H.Richards, J.R.Winkler, and H.B.Gray (2008).
Tryptophan-accelerated electron flow through proteins.
  Science, 320, 1760-1762.
PDB code: 2i7o
  19262679 K.Yokoyama, B.S.Leigh, Y.Sheng, K.Niki, N.Nakamura, H.Ohno, J.R.Winkler, H.B.Gray, and J.H.Richards (2008).
Electron Tunneling through Pseudomonas aeruginosa Azurins on SAM Gold Electrodes.
  Inorganica Chim Acta, 361, 1095-1099.  
18092096 N.Yokoi, T.Ueno, M.Unno, T.Matsui, M.Ikeda-Saito, and Y.Watanabe (2008).
Ligand design for the improvement of stability of metal complex.protein hybrids.
  Chem Commun (Camb), (), 229-231.
PDB code: 2z68
18314977 R.Sarangi, S.I.Gorelsky, L.Basumallick, H.J.Hwang, R.C.Pratt, T.D.Stack, Y.Lu, K.O.Hodgson, B.Hedman, and E.I.Solomon (2008).
Spectroscopic and density functional theory studies of the blue-copper site in M121SeM and C112SeC azurin: Cu-Se versus Cu-S bonding.
  J Am Chem Soc, 130, 3866-3877.  
17301232 C.Zong, C.J.Wilson, T.Shen, P.Wittung-Stafshede, S.L.Mayo, and P.G.Wolynes (2007).
Establishing the entatic state in folding metallated Pseudomonas aeruginosa azurin.
  Proc Natl Acad Sci U S A, 104, 3159-3164.  
17609782 M.Razavet, V.Artero, C.Cavazza, Y.Oudart, C.Lebrun, J.C.Fontecilla-Camps, and M.Fontecave (2007).
Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic protein.
  Chem Commun (Camb), (), 2805-2807.
PDB code: 2q0m
17167808 P.Haquette, M.Salmain, K.Svedlung, A.Martel, B.Rudolf, J.Zakrzewski, S.Cordier, T.Roisnel, C.Fosse, and G.Jaouen (2007).
Cysteine-specific, covalent anchoring of transition organometallic complexes to the protein papain from Carica papaya.
  Chembiochem, 8, 224-231.  
16651527 C.Li, S.Yanagisawa, B.M.Martins, A.Messerschmidt, M.J.Banfield, and C.Dennison (2006).
Basic requirements for a metal-binding site in a protein: the influence of loop shortening on the cupredoxin azurin.
  Proc Natl Acad Sci U S A, 103, 7258-7263.
PDB codes: 2ft6 2ft7 2ft8 2fta
17179046 M.Cascella, A.Magistrato, I.Tavernelli, P.Carloni, and U.Rothlisberger (2006).
Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa.
  Proc Natl Acad Sci U S A, 103, 19641-19646.  
16234922 C.Dennison (2005).
Ligand and loop variations at type 1 copper sites: influence on structure and reactivity.
  Dalton Trans, (), 3436-3442.  
15738403 H.B.Gray, and J.R.Winkler (2005).
Long-range electron transfer.
  Proc Natl Acad Sci U S A, 102, 3534-3539.  
15987900 L.A.Alcaraz, B.Jiménez, J.M.Moratal, and A.Donaire (2005).
An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloprotein.
  Protein Sci, 14, 1710-1722.  
15726624 M.Babor, H.M.Greenblatt, M.Edelman, and V.Sobolev (2005).
Flexibility of metal binding sites in proteins on a database scale.
  Proteins, 59, 221-230.  
16260751 Q.Chi, O.Farver, and J.Ulstrup (2005).
Long-range protein electron transfer observed at the single-molecule level: In situ mapping of redox-gated tunneling resonance.
  Proc Natl Acad Sci U S A, 102, 16203-16208.  
16227441 S.A.Kang, and B.R.Crane (2005).
Effects of interface mutations on association modes and electron-transfer rates between proteins.
  Proc Natl Acad Sci U S A, 102, 15465-15470.
PDB codes: 2b0z 2b10 2b11 2b12
12657732 H.B.Gray (2003).
Biological inorganic chemistry at the beginning of the 21st century.
  Proc Natl Acad Sci U S A, 100, 3563-3568.  
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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