Please use this identifier to cite or link to this item:
Title: Resonance raman and FTIR studies of carbon monoxide-bound cytochrome aa3-600 oxidase of bacillus subtilis
Authors: Vamvouka, Magdalini
Varotsis, Constantinos 
Keywords: Fourier transform infrared spectroscopy;Carbon;Cytochrome oxidase;Bacillus subtilis;Heme;Ligands;Chemistry
Issue Date: 1998
Publisher: ACS Publications
Source: Journal of physical chemistry B, 1998, volume 102, issue 39, pages 7670-7673
Abstract: Resonance Raman and FTIR spectra are reported for the fully reduced carbon monoxy derivative of the quinol aa3-600 oxidase from Bacillus subtilis. The resonance Raman spectra display two isotope-dependent vibrational modes at 520 and 575 cm-1. The FTIR spectrum displays a single vibrational mode at 1963 cm-1. We assign the band at 520 cm-1 to the Fe-CO stretching mode, the band at 575 cm-1 to the Fe-C-O bending mode, and the band at 1963 cm-1 to the C-O stretching mode. The frequencies of these modes are similar to those that have been reported for the CO-bound mammalian cytochrome c oxidase. Despite the fact that two different heme-protein conformations that affect the iron-his bond strength are present in the ferrous ligand-free form of aa3-600, the CO-bound adduct has a single conformation in which the His-Fe-CO CUB moiety has the same structure as the α form found in the mammalian cytochrome c oxidase. The present and previous data on the vibrational frequencies of ferrous ligand-free and ferrous CO-bound forms of terminal oxidases show that an inverse linear relationship exists between the frequencies of the Fe-his and Fe-CO stretching modes. We suggest that the frequencies of both the Fe-CO and C-O modes found in heme-CUB oxidases are affected by the proximal His376, which is H-bonded to the peptide carbonyl of Gly351, and by distal effects on the heme a3-bound CO exerted by CuB
ISSN: 10895647
DOI: 10.1021/jp9824095
Rights: Copyright © 1998 American Chemical Society
Type: Article
Appears in Collections:Άρθρα/Articles

Show full item record

Citations 20

checked on Oct 16, 2019

Page view(s) 20

Last Week
Last month
checked on Oct 21, 2019

Google ScholarTM



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