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1jzg
From Proteopedia
(New page: 200px<br /><applet load="1jzg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jzg, resolution 1.40Å" /> '''Pseudomonas aerugino...) |
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| - | [[Image:1jzg.gif|left|200px]]<br /><applet load="1jzg" size=" | + | [[Image:1jzg.gif|left|200px]]<br /><applet load="1jzg" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jzg, resolution 1.40Å" /> | caption="1jzg, resolution 1.40Å" /> | ||
'''Pseudomonas aeruginosa Reduced Azurin (Cu1+) Ru(tpy)(phen)(His83)'''<br /> | '''Pseudomonas aeruginosa Reduced Azurin (Cu1+) Ru(tpy)(phen)(His83)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Rates of reduction of Os(III), Ru(III), and Re(I) by Cu(I) in | + | 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 Structure== | ==About this Structure== | ||
| - | 1JZG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with CU1, RTB and IMF as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1JZG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=CU1:'>CU1</scene>, <scene name='pdbligand=RTB:'>RTB</scene> and <scene name='pdbligand=IMF:'>IMF</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZG OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bilio, A | + | [[Category: Bilio, A J.Di.]] |
| - | [[Category: Crane, B | + | [[Category: Crane, B R.]] |
| - | [[Category: Gray, H | + | [[Category: Gray, H B.]] |
| - | [[Category: Winkler, J | + | [[Category: Winkler, J R.]] |
[[Category: CU1]] | [[Category: CU1]] | ||
[[Category: IMF]] | [[Category: IMF]] | ||
| Line 24: | Line 24: | ||
[[Category: ruthenium]] | [[Category: ruthenium]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:25 2008'' |
Revision as of 11:28, 21 February 2008
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Pseudomonas aeruginosa Reduced Azurin (Cu1+) Ru(tpy)(phen)(His83)
Overview
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 Structure
1JZG is a Single protein structure of sequence from Pseudomonas aeruginosa with , and as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 13:28:25 2008
