Please use this identifier to cite or link to this item: http://ktisis.cut.ac.cy/handle/10488/6598
Title: Resonance Raman detection of the Fe2+-C-N modes in heme-copper oxidases: a probe of the active site
Authors: Pinakoulaki, Eftychia 
Vamvouka, Magdalini
Varotsis, Constantinos 
Keywords: Copper;Heme;Iron;Cattle;Raman spectrometry;Vibration;Enzymes;Cytochromes;Spectrum analysis
Issue Date: 2004
Publisher: ACS Publications
Source: Inorganic chemistry, 2004, Volume 43, Issue 16, Pages 4907-4910
Abstract: Resonance Raman spectroscopy has been employed to investigate the reduced cyano complexes of cytochrome aa3 from bovine heart and Rhodobacter sphaeroides and of cytochrome bo3 from E. coli. In the aa 3-type oxidases, the frequency of the Fe-CN stretching mode is located at 468 cm-1, and the bending Fe-C-N vibration, at 500 cm -1. The fully reduced cytochrome bo3-CN complex gives rise to a stretching vibration at 468 cm-1, a bending vibration at 491 cm-1, and a stretching C-N vibration at 2037 cm-1. The observed differences between aa3 and bo3 oxidases in the frequencies of the Fe-C-N group suggest a quantitative difference in the structure of the His-heme a32+/CuB1+ and His-heme o32+/CuB1+ binuclear pockets upon CN- binding
URI: http://ktisis.cut.ac.cy/handle/10488/6598
ISSN: 00201669
DOI: 10.1021/ic035216r
Rights: Copyright © 2004 American Chemical Society
Type: Article
Appears in Collections:Άρθρα/Articles

Show full item record

SCOPUSTM   
Citations 20

9
checked on Nov 16, 2017

WEB OF SCIENCETM
Citations 10

8
checked on Nov 16, 2017

Page view(s)

23
Last Week
1
Last month
0
checked on Nov 19, 2017

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.