English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The Herbicide Resistant Mutant T1 from Rhodopseudomonasviridis Altered Herbicide Binding and Three-Dimensional Structure

Sinning, I. M., Koepke, J., Schiller, B., Mathies, P., Rutherford, A., & Michel, H. (1990). The Herbicide Resistant Mutant T1 from Rhodopseudomonasviridis Altered Herbicide Binding and Three-Dimensional Structure. Springer, Dordrecht: Springer Science+Business Media B.V. 1990.

Item is

Basic

show hide
Genre: Conference Paper

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Sinning, Irmgard Maria1, Author              
Koepke, Jürgen1, Author              
Schiller, Barbara1, Author              
Mathies, P.2, Author
Rutherford, A.W.2, Author
Michel, Hartmut1, Author              
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Service de Biophysique, Dep. de Biologie, C.E.N. Saclay, Gif-sur-Yvette, Cedex, France, ou_persistent22              

Content

show
hide
Free keywords: Purple Bacterium; Photosynthetic Reaction Center; Triazine Ring; Significant Sequence Homology; Hydroxo Group
 Abstract: Herbicides of the triazine class are known to act by competing with the secondary acceptor, QB, for binding to the photosynthetic reaction center (RC) of purple bacteria and PSII (1,2). The binding of terbutryn to the RC of the purple bacterium Rhodopseudomonas (Rps.) viridis wild type (WT) was established by X-ray crystallography (3). Several hydrogen bonds and numerous van der Waals interactions contribute to the binding of the inhibitor. There is a hydrogen bond possible between the ethylamino group of terbutryn and the hydroxo group of serine L223. A second hydrogen bond is likely between a nitrogen atom of the triazine ring and the peptide nitrogen of isoleucine L224. Several mutants, which are resistant toward terbutryn, have been isolated by selecting for photosynthetic growth in the presence of the herbicide (4,5). In the mutant Tl (SerL223→Ala and Arg L217→His) binding of the secondary acceptor, QB, is increased compared to the wild type (5). Due to significant sequence homologies, structural and mechanistic similarities, the RC of purple bacteria is an interesting model for PSII

Details

show
hide
Language(s): eng - English
 Dates: 1990
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1007/978-94-009-0511-5_37
 Degree: -

Event

show
hide
Title: Proceedings of the VIIIth International Conference on Photosynthesis
Place of Event: Stockholm, Sweden
Start-/End Date: 1989-08-06 - 1989-08-11
Invited: Yes

Legal Case

show

Project information

show

Source 1

show
hide
Title: Current Research in Photosynthesis
Source Genre: Series
 Creator(s):
Baltscheffsky, M.1, Editor
Affiliations:
1 Department of Biochemistry, University of Stockholm, Stockholm, Sweden, ou_persistent22            
Publ. Info: Springer, Dordrecht : Springer Science+Business Media B.V. 1990
Pages: - Volume / Issue: 1 Sequence Number: - Start / End Page: 173 - 176 Identifier: DOI: 10.1007/978-94-009-0511-5
ISBN: 978-94-010-6716-4
ISBN: 978-94-009-0511-5