Document Detail


Use of 3-aminotyrosine to examine the pathway dependence of radical propagation in Escherichia coli ribonucleotide reductase.
MedLine Citation:
PMID:  19916558     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Escherichia coli ribonucleotide reductase (RNR), an alpha2beta2 complex, catalyzes the conversion of nucleoside 5'-diphosphate substrates (S) to 2'-deoxynucleoside 5'-diphosphates. alpha2 houses the active site for nucleotide reduction and the binding sites for allosteric effectors (E). beta2 contains the essential diferric tyrosyl radical (Y(122)(*)) cofactor which, in the presence of S and E, oxidizes C(439) in alpha to a thiyl radical, C(439)(*), to initiate nucleotide reduction. This oxidation occurs over 35 A and is proposed to involve a specific pathway: Y(122)(*) --> W(48) --> Y(356) in beta2 to Y(731) --> Y(730) --> C(439) in alpha2. 3-Aminotyrosine (NH(2)Y) has been site-specifically incorporated at residues 730 and 731, and formation of the aminotyrosyl radical (NH(2)Y(*)) has been examined by stopped-flow (SF) UV-vis and EPR spectroscopies. To examine the pathway dependence of radical propagation, the double mutant complexes Y(356)F-beta2:Y(731)NH(2)Y-alpha2, Y(356)F-beta2:Y(730)NH(2)Y-alpha2, and wt-beta2:Y(731)F/Y(730)NH(2)Y-alpha2, in which the nonoxidizable F acts as a pathway block, were studied by SF and EPR spectroscopies. In all cases, no NH(2)Y(*) was detected. To study off-pathway oxidation, Y(413), located 5 A from Y(730) and Y(731) but not implicated in long-range oxidation, was examined. Evidence for NH(2)Y(413)(*) was sought in three complexes: wt-beta2:Y(413)NH(2)Y-alpha2 (a), wt-beta2:Y(731)F/Y(413)NH(2)Y-alpha2 (b), and Y(356)F-beta2:Y(413)NH(2)Y-alpha2 (c). With (a), NH(2)Y(*) was formed with a rate constant that was 25-30% and an amplitude that was 25% of that observed for its formation at residues 731 and 730. With (b), the rate constant for NH(2)Y(*) formation was 0.2-0.3% of that observed at 731 and 730, and with (c), no NH(2)Y(*) was observed. These studies suggest the evolution of an optimized pathway of conserved Ys in the oxidation of C(439).
Authors:
Ellen C Minnihan; Mohammad R Seyedsayamdost; JoAnne Stubbe
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemistry     Volume:  48     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2009 Dec 
Date Detail:
Created Date:  2009-12-22     Completed Date:  2010-01-12     Revised Date:  2011-08-01    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  12125-32     Citation Subset:  IM    
Affiliation:
Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge,Massachusetts 02139-4307, USA.
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MeSH Terms
Descriptor/Qualifier:
Electron Spin Resonance Spectroscopy
Electron Transport
Escherichia coli / chemistry*,  genetics,  metabolism
Escherichia coli Proteins / chemistry*,  genetics,  metabolism
Free Radicals / chemistry*
Oxidation-Reduction
Ribonucleoside Diphosphate Reductase / chemistry*,  genetics,  metabolism
Tyrosine / analogs & derivatives*,  chemistry
Grant Support
ID/Acronym/Agency:
GM29595/GM/NIGMS NIH HHS; R01 GM029595-30/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Free Radicals; 300-34-5/3-aminotyrosine; 55520-40-6/Tyrosine; EC 1.17.4.1/Ribonucleoside Diphosphate Reductase

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