1jzf

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(New page: 200px<br /><applet load="1jzf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jzf, resolution 1.50&Aring;" /> '''Pseudomonas aerugino...)
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[[Image:1jzf.gif|left|200px]]<br /><applet load="1jzf" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jzf.gif|left|200px]]<br /><applet load="1jzf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jzf, resolution 1.50&Aring;" />
caption="1jzf, resolution 1.50&Aring;" />
'''Pseudomonas aeruginosa Oxidized Azurin(Cu2+) Ru(tpy)(phen)(His83)'''<br />
'''Pseudomonas aeruginosa Oxidized Azurin(Cu2+) Ru(tpy)(phen)(His83)'''<br />
==Overview==
==Overview==
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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) --&gt; 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.
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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) --&gt; 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==
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1JZF 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 CU, RTB and IME as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JZF OCA].
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1JZF 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=CU:'>CU</scene>, <scene name='pdbligand=RTB:'>RTB</scene> and <scene name='pdbligand=IME:'>IME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZF OCA].
==Reference==
==Reference==
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Bilio, A.J.Di.]]
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[[Category: Bilio, A J.Di.]]
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[[Category: Crane, B.R.]]
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[[Category: Crane, B R.]]
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[[Category: Gray, H.B.]]
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[[Category: Gray, H B.]]
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[[Category: Winkler, J.R.]]
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[[Category: Winkler, J R.]]
[[Category: CU]]
[[Category: CU]]
[[Category: IME]]
[[Category: IME]]
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[[Category: tunneling]]
[[Category: tunneling]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:43:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:30 2008''

Revision as of 11:28, 21 February 2008

Image:1jzf.gif

1jzf, resolution 1.50Å

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Pseudomonas aeruginosa Oxidized Azurin(Cu2+) 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

1JZF 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

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