We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1jze

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jze.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1jze.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jze| PDB=1jze | SCENE= }}
{{STRUCTURE_1jze| PDB=1jze | SCENE= }}
-
'''Pseudomonas aeruginosa Azurin Ru(bpy)2(im)(His83)'''
+
===Pseudomonas aeruginosa Azurin Ru(bpy)2(im)(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) --&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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11716717}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11716717 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11716717}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Electron transfer]]
[[Category: Electron transfer]]
[[Category: Ruthenium]]
[[Category: Ruthenium]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:06:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:42:12 2008''

Revision as of 13:42, 28 July 2008

Image:1jze.png

Template:STRUCTURE 1jze

Pseudomonas aeruginosa Azurin Ru(bpy)2(im)(His83)

Template:ABSTRACT PUBMED 11716717

About this Structure

1JZE is a Single protein structure of sequence from Pseudomonas aeruginosa. 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 Mon Jul 28 16:42:12 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jze"
Personal tools