English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Direct Evidence for the Interaction of Stigmatellin with a Protonated Acidic Group in the bc1 Complex from Saccharomyces cerevisiae As Monitored by FTIR Difference Spectroscopy and 13C Specific Labeling.

Ritter, M., Palsdottir, H., Abe, M., Mäntele, W., Hunte, C., Miyoshi, H., et al. (2004). Direct Evidence for the Interaction of Stigmatellin with a Protonated Acidic Group in the bc1 Complex from Saccharomyces cerevisiae As Monitored by FTIR Difference Spectroscopy and 13C Specific Labeling. Biochemistry, 43, 8439-8446. doi:10.1021/bi049649x.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-DAD2-4 Version Permalink: http://hdl.handle.net/21.11116/0000-0007-A7C2-1
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Ritter, Michaela1, Author
Palsdottir, Hildur2, Author              
Abe, Masato3, Author
Mäntele, Werner1, Author
Hunte, Carola2, Author              
Miyoshi, Hideto3, Author
Hellwig, Petra1, Author
Affiliations:
1Institut für Biophysik, Johann Wolfgang Goethe-Universität Frankfurt, 60590 Frankfurt am Main, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan , ou_persistent22              

Content

show
hide
Free keywords: Bioinorganic chemistry; Peptides and proteins; Reaction mechanisms; Fourier transform infrared spectroscopy; Inhibitors
 Abstract: In this study a combined electrochemical and FTIR spectroscopic approach was applied to monitor the binding of stigmatellin, a Qo site inhibitor of the cytochrome bc1 complex from Saccharomyces cerevisiae. Natural stigmatellin A induced clear shifts in the redox-induced FTIR difference spectra. For data interpretation a stigmatellin derivative (UST) with the conjugated trienes replaced by an aliphatic tail was synthesized, and the carbonyl group shown in crystal structures to interact with His181, the [2Fe-2S] ligand of the Rieske, was specifically 13C labeled. Electrochemically induced FTIR difference spectra of the inhibitors in CH3OD were obtained and revealed signals characteristic for the oxidized and reduced forms of the labeled and unlabeled compounds. On the basis of signals from the inhibitors alone, the binding of the inhibitor to the bc1 complex was monitored. Direct evidence for the interaction of the carbonyl group with the protein was provided by the observed shift of the ν(CO) vibrational mode of about 10 cm-1. In addition, redox-dependent reorganizations of the protein were identified, including protonation changes of acidic residues at 1746 and 1734 cm-1. The conformational changes observed upon inhibitor binding are discussed with respect to the crystal structures and proposed mechanistic models [Hunte, C., Koepke, J., Lange, C., Rossmanith, T., and Michel, H. (2000) Structure 8, 669−684; Palsdottir, H., Lojero, C. G., Trumpower, B. L., and Hunte, C. (2003) J. Biol. Chem. 278, 31303−31311].

Details

show
hide
Language(s): eng - English
 Dates: 2004-04-212004-02-172004-06-092004-07-01
 Publication Status: Published in print
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi049649x
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemistry
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 43 Sequence Number: - Start / End Page: 8439 - 8446 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103