English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  An uncharged amine in the transition state of the ribosornal peptidyl transfer reaction.

Kingery, D. A., Pfund, E., Voorhees, R. M., Okuda, K., Wohlgemuth, I., Kitchen, D. E., et al. (2008). An uncharged amine in the transition state of the ribosornal peptidyl transfer reaction. Chemistry and Biology, 15(5), 493-500. Retrieved from http://download.cell.com/chemistry-biology/pdf/PIIS1074552108001555.pdf.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-DC35-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-8305-8
Genre: Journal Article

Files

show Files
hide Files
:
588703.pdf (Publisher version), 306KB
Name:
588703.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Kingery, D. A., Author
Pfund, E., Author
Voorhees, R. M., Author
Okuda, K., Author
Wohlgemuth, I.1, Author              
Kitchen, D. E., Author
Rodnina, M. V.1, Author              
Strobel, S. A., Author
Affiliations:
1Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578598              

Content

show
hide
Free keywords: -
 Abstract: The ribosome has an active site comprised of RNA that catalyzes peptide bond formation. To understand how RNA promotes this reaction requires a detailed understanding of the chemical transition state. Here, we report the Bronsted coefficient of the a-amino nucleophile with a series of puromycin derivatives. Both 50S subunit- and 70S ribosome-catalyzed reactions displayed linear free-energy relationships with slopes close to zero under conditions where chemistry is rate limiting. These results indicate that, at the transition state, the nucleophile is neutral in the ribosome-catalyzed reaction, in contrast to the substantial positive charge reported for typical uncatalyzed aminolysis reactions. This suggests that the ribosomal transition state involves deprotonation to a degree commensurate with nitrogen-carbon bond formation. Such a transition state is significantly different from that of uncatalyzed aminolysis reactions in solution.

Details

show
hide
Language(s): eng - English
 Dates: 2008-05
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Chemistry and Biology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 15 (5) Sequence Number: - Start / End Page: 493 - 500 Identifier: -