Please use this identifier to cite or link to this item:
https://hdl.handle.net/20.500.14279/1049
Title: | Resonance raman and FTIR studies of carbon monoxide-bound cytochrome aa3-600 oxidase of bacillus subtilis | Authors: | Vamvouka, Magdalini Varotsis, Constantinos |
metadata.dc.contributor.other: | Βάμβουκα, Μαγδαληνή Βαρώτσης, Κωνσταντίνος |
Major Field of Science: | Engineering and Technology | Keywords: | Fourier transform infrared spectroscopy;Carbon;Cytochrome oxidase;Bacillus subtilis;Heme;Ligands;Chemistry | Issue Date: | 9-Sep-1998 | Source: | Journal of Physical Chemistry B, 1998, vol. 102, no. 39, pp. 7670-7673 | Volume: | 102 | Issue: | 39 | Start page: | 7670 | End page: | 7673 | Journal: | Journal of Physical Chemistry B | 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 | URI: | https://hdl.handle.net/20.500.14279/1049 | ISSN: | 10895647 | DOI: | 10.1021/jp9824095 | Rights: | © American Chemical Society | Type: | Article | Affiliation: | University of Crete | Affiliation : | University of Crete |
Appears in Collections: | Άρθρα/Articles |
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