1jzi: Difference between revisions
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|PDB= 1jzi |SIZE=350|CAPTION= <scene name='initialview01'>1jzi</scene>, resolution 1.62Å | |PDB= 1jzi |SIZE=350|CAPTION= <scene name='initialview01'>1jzi</scene>, resolution 1.62Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=REP:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REP | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=IME:TETRA(IMIDAZOLE)DIAQUACOPPER+(II)'>IME</scene>, <scene name='pdbligand=REP:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REP</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1jze|1JZE]], [[1jzf|1JZF]], [[1jzg|1JZG]], [[1jzh|1JZH]], [[1jzj|1JZJ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jzi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jzi OCA], [http://www.ebi.ac.uk/pdbsum/1jzi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jzi RCSB]</span> | |||
}} | }} | ||
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[[Category: Gray, H B.]] | [[Category: Gray, H B.]] | ||
[[Category: Winkler, J R.]] | [[Category: Winkler, J R.]] | ||
[[Category: blue-copper]] | [[Category: blue-copper]] | ||
[[Category: electron-transfer]] | [[Category: electron-transfer]] | ||
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[[Category: tunneling]] | [[Category: tunneling]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:41:11 2008'' | ||
Revision as of 21:41, 30 March 2008
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| , resolution 1.62Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Related: | 1JZE, 1JZF, 1JZG, 1JZH, 1JZJ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Pseudomonas aeruginosa Azurin Re(phen)(CO)3(His83)
OverviewOverview
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.
About this StructureAbout this Structure
1JZI is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
ReferenceReference
Electron tunneling in single crystals of Pseudomonas aeruginosa azurins., Crane BR, Di Bilio AJ, Winkler JR, Gray HB, J Am Chem Soc. 2001 Nov 28;123(47):11623-31. PMID:11716717
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