Home | My Profile | Contact Us
Research Trends Products  |   order gateway  |   author gateway  |   editor gateway  
Register | Forgot Password

Author Resources
 Author Gateway
 Article submission guidelines

Editor Resources
 Editor/Referee Gateway

 Regional Subscription Agents/Distributors
Trends in Comparative Biochemistry & Physiology   Volumes    Volume 9 
Mechanism of quinol oxidation in cytochrome bc1 complex
Rafael Moreno-Sanchez, Raul Covian
Pages: 17 - 32
Number of pages: 16
Trends in Comparative Biochemistry & Physiology
Volume 9 

Copyright © 2002 Research Trends. All rights reserved


The cytochrome bc1 complex is one of the enzymes that couples electron transfer to vectorial proton translocation in energy-transducing biomembranes. It is also one of the main sources of reactive oxygen species in the cell, and an early target for apoptosis-inducing molecules. Energy conservation in this complex is made possible by the obliged bifurcation of the electrons derived from quinol oxidation. Different models have been proposed to explain the mechanism which ensures this electron bifurcation. Some of these models consider that two quinone molecules occupy the quinol oxidation (Qo) site, while others propose the movement of a single quinone within the two domains that comprise this site. Crystallographic structures and mutational studies have shown the existence of movement of the soluble domain of the iron-sulfur protein (ISP), modifying previous models and generating new ones that assign to this movement a mechanistic role in electron bifurcation. In this review, the evidence supporting the different models of quinol oxidation in the bc1 complex is critically analyzed.

Buy this Article


Buy this article
Buy this volume
Subscribe to this title
Shopping Cart

Quick Links
Search Products
Browse in Alphabetical Order : Journals
Browse by Subject Classification : Journals

Ordering Information Ordering Information
Downloadable forms Downloadable Forms