{"controller"=>"catalog", "action"=>"show", "id"=>"241113480"}
  • EN
  • DA

Danish NationalResearch Database

  • Search Publications & Researchers
  • Open Access Indicator
  • Publications
  • Researchers
Example Finds records
water{} containing the word "water".
water supplies"{}" containing the phrase "water supplies".
author:"Doe, John"author:"{}" containing the prase "Doe, John" in the author field.
title:IEEEtitle:{} containing the word "IEEE" in the title field.
Need more help? Advanced search tutorial
  • Selected (0)
  • History

Key role of water in proton transfer at the Q(o)-site of the cytochrome bc(1) complex predicted by atomistic molecular dynamics simulations

    • Save to Mendeley
    • Export to BibTeX
    • Export to RIS
    • Email citation
Authors:
  • Postila, P. A. ;
    Close
    unknown
  • Kaszuba, K. ;
    Close
    unknown
  • Sarewicz, M. ;
    Close
    unknown
  • Osyczka, A. ;
    Close
    unknown
  • Vattulainen, I. ;
    Close
    Department of Physics, Chemistry and Pharmacy, Faculty of Science, SDU
  • Rog, T.
    Close
    unknown
DOI:
10.1016/j.bbabio.2013.02.005
Abstract:
Cytochrome (cyt) bc(1) complex, which is an integral part of the respiratory chain and related energy-conserving systems, has two quinone-binding cavities (Q(o)- and Q(i)-sites), where the substrate participates in electron and proton transfer. Due to its complexity, many of the mechanistic details of the cyt bc(1) function have remained unclear especially regarding the substrate binding at the Q(o)-site. In this work we address this issue by performing extensive atomistic molecular dynamics simulations with the cyt bc(1) complex of Rhodobacter capsulatus embedded in a lipid bilayer. Based on the simulations we are able to show the atom-level binding modes of two substrate forms: quinol (QH(2)) and quinone (Q). The QH(2) binding at the Q(o)-site involves a coordinated water arrangement that produces an exceptionally close and stable interaction between the cyt b and iron sulfur protein subunits. In this arrangement water molecules are positioned suitably in relation to the hydroxyls of the QH(2) ring to act as the primary acceptors of protons detaching from the oxidized substrate. In contrast, water does not have a similar role in the Q binding at the Q(o)-site. Moreover, the coordinated water molecule is also a prime candidate to act as a structural element, gating for short-circuit suppression at the Q(o)-site. (c) 2013 Elsevier B.V. All rights reserved.
Type:
Journal article
Language:
English
Published in:
B B a - Bioenergetics, 2013, Vol 1827, Issue 6, p. 761-768
Keywords:
Cytochrome bc(1) Molecular dynamics simulation Quinol/quinone Electron transfer Proton transfer Short-circuit suppression ELECTRON-TRANSFER CHAINS IRON-SULFUR PROTEIN Q(O) SITE Q-CYCLE SACCHAROMYCES-CEREVISIAE UBIQUINOL OXIDATION RESPIRATORY-CHAIN QUINOL OXIDATION LIGAND-BINDING BOVINE HEART
Main Research Area:
Science/technology
Publication Status:
Published
Review type:
Peer Review
Submission year:
2013
Scientific Level:
Scientific
ID:
241113480

Full text access

  • Doi Get publisher edition via DOI resolver
Checking for on-site access...

On-site access

At institution

  • University southern denmark

Metrics

Feedback

Sitemap

  • Search
    • Statistics
    • Tutorial
    • Data
    • FAQ
    • Contact
  • Open Access
    • Overview
    • Development
    • FAQ
    • Contact
  • About
    • Institutions
    • Release History
    • Cookies and privacy policy

Copyright © 1998–2018.

Fivu en