2rdb: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
Line 1: Line 1:
[[Image:2rdb.jpg|left|200px]]
{{Seed}}
[[Image:2rdb.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rdb|  PDB=2rdb  |  SCENE=  }}  
{{STRUCTURE_2rdb|  PDB=2rdb  |  SCENE=  }}  


'''X-ray Crystal Structure of Toluene/o-Xylene Monooxygenase Hydroxylase I100W Mutant'''
===X-ray Crystal Structure of Toluene/o-Xylene Monooxygenase Hydroxylase I100W Mutant===




==Overview==
<!--  
At its carboxylate-bridged diiron active site, the hydroxylase component of toluene/o-xylene monooxygenase activates dioxygen for subsequent arene hydroxylation. In an I100W variant of this enzyme, we characterized the formation and decay of two species formed by addition of dioxygen to the reduced, diiron(II) state by rapid-freeze quench (RFQ) EPR, Mossbauer, and ENDOR spectroscopy. The dependence of the formation and decay rates of this mixed-valent transient on pH and the presence of phenol, propylene, or acetylene was investigated by double-mixing stopped-flow optical spectroscopy. Modification of the alpha-subunit of the hydroxylase after reaction of the reduced protein with dioxygen-saturated buffer was investigated by tryptic digestion coupled mass spectrometry. From these investigations, we conclude that (i) a diiron(III,IV)-W* transient, kinetically linked to a preceding diiron(III) intermediate, arises from the one-electron oxidation of W100, (ii) the tryptophan radical is deprotonated, (iii) rapid exchange of either a terminal water or hydroxide ion with water occurs at the ferric ion in the diiron(III,IV) cluster, and (iv) the diiron(III,IV) core and W* decay to the diiron(III) product by a common mechanism. No transient radical was observed by stopped-flow optical spectroscopy for reactions of the reduced hydroxylase variants I100Y, L208F, and F205W with dioxygen. The absence of such species, and the deprotonated state of the tryptophanyl radical in the diiron(III,IV)-W* transient, allow for a conservative estimate of the reduction potential of the diiron(III) intermediate as lying between 1.1 and 1.3 V. We also describe the X-ray crystal structure of the I100W variant of ToMOH.
The line below this paragraph, {{ABSTRACT_PUBMED_18044971}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 18044971 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_18044971}}


==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Tryptophan radical]]
[[Category: Tryptophan radical]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:07:43 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:16:29 2008''

Revision as of 02:16, 28 July 2008

File:2rdb.png

Template:STRUCTURE 2rdb

X-ray Crystal Structure of Toluene/o-Xylene Monooxygenase Hydroxylase I100W Mutant

Template:ABSTRACT PUBMED 18044971

About this Structure

2RDB is a Protein complex structure of sequences from Pseudomonas stutzeri. Full crystallographic information is available from OCA.

Reference

Dioxygen activation at non-heme diiron centers: oxidation of a proximal residue in the I100W variant of toluene/o-xylene monooxygenase hydroxylase., Murray LJ, Garcia-Serres R, McCormick MS, Davydov R, Naik SG, Kim SH, Hoffman BM, Huynh BH, Lippard SJ, Biochemistry. 2007 Dec 25;46(51):14795-809. Epub 2007 Nov 29. PMID:18044971

Page seeded by OCA on Mon Jul 28 05:16:29 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2rdb&oldid=682871"