NISCAIR Online Periodicals Repository

Research Journals >
Indian Journal of Chemistry -Section A (IJC-A) >
IJC-A Vol.50A [2011] >
IJC-A Vol.50A(03-04) [March-April 2011] >

Title: Bacterial model systems for cytochrome c oxidase biogenesis
Authors: Hannappel, A
Bundschuh, F A
Greiner, P
Alles, M
Werner, C
Richter, O M
Ludwig, B
Keywords: Bioinorganic chemistry
Oxidase assembly
Terminal oxidase
Heme copper oxidase
Chaperone proteins
Heme a
Issue Date: Mar-2011
Publisher: NISCAIR-CSIR, India
Abstract: Cytochrome c oxidase is the key player in cellular respiration, catalysing the reduction of molecular oxygen to water via its internal heme and copper redox centres. Biogenesis of the enzyme is a complex process involving up to 30 accessory proteins in higher eukaryotes. Factors directly involved in cofactor recruitment and insertion into the two core structural subunits I and II are also present in many bacteria and have been conserved during evolution. Herein we briefly review the chaperones required during early biogenesis steps, with special emphasis on the bacterial counterparts.
Page(s): 374-382
CC License:  CC Attribution-Noncommercial-No Derivative Works 2.5 India
ISSN: 0975-0975(Online); 0376-4710(Print)
Source:IJC-A Vol.50A(03-04) [March-April 2011]

Files in This Item:

File Description SizeFormat
IJCA 50A(03-04) 374-382.pdf261.83 kBAdobe PDFView/Open
 Current Page Visits: 210 
Recommend this item


Online Submission of Articles |  NISCAIR Website |  National Knowledge Resources Consortium |  Contact us |  Feedback

Disclaimer: NISCAIR assumes no responsibility for the statements and opinions advanced by contributors. The editorial staff in its work of examining papers received for publication is helped, in an honorary capacity, by many distinguished engineers and scientists.

CC License Except where otherwise noted, the Articles on this site are licensed under Creative Commons License: CC Attribution-Noncommercial-No Derivative Works 2.5 India

Copyright © 2015 The Council of Scientific and Industrial Research, New Delhi. All rights reserved.

Powered by DSpace Copyright © 2002-2007 MIT and Hewlett-Packard | Compliant to OAI-PMH V 2.0

Home Page Total Visits: 167209 since 01-Sep-2015  Last updated on 28-Jun-2016Webmaster: