English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Book Chapter

Crystallization of Wolinella succinogenes quinol:fumarate reductase

MPS-Authors
/persons/resource/persons137768

Lancaster,  C. Roy D.
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Ressource
No external resources are shared
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

Lancaster, C. R. D. (2003). Crystallization of Wolinella succinogenes quinol:fumarate reductase. In C. Hunte, G. von Jagow, & H. Schägger (Eds.), Membrane Protein Purification and Crystallization: A Practical Guide. (2nd edition, pp. 219-228). San Diego/USA: Academic Press Inc. doi:10.1016/B978-012361776-7/50014-0.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-DB47-3
Abstract
INTRODUCTION Quinol:fumarate reductases (QFR) and succinate:quinone reductases (SQR) catalyze the reduction of fumarate to succinate with concomitant oxidation of hydroquinone (quinol) to quinone, as well as the reverse reaction. SQR (respiratory complex II) is involved in aerobic metabolism as part of the citric acid cycle and the aerobic respiratory chain. QFR is involved in anaerobic respiration with fumarate as the terminal electron acceptor (Kröger, 1978; Kröger et al., 1992), and it is part of the electron transport chain catalyzing the oxidation of various donor substrates (e.g., NADH, H2 or formate) by fumarate. These reactions are coupled to ADP phosphorylation via an electrochemical proton potential.