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https://hdl.handle.net/20.500.14279/1921
Title: | Detection of a photostable five-coordinate heme a3-Fe-Co species and functional implications of His384/α10 in CO-bound ba 3-cytochrome c oxidase from Thermus thermophilus |
Authors: | Pinakoulaki, Eftychia Ohta, Takehiro Varotsis, Constantinos |
metadata.dc.contributor.other: | Πινακουλάκη, Ευτυχία Βαρώτσης, Κωνσταντίνος |
Major Field of Science: | Engineering and Technology |
Field Category: | Chemical Engineering |
Keywords: | Stereochemistry;Cadmium compounds;Carbon monoxide;Copper;Enzymes;Iron compounds;Mercury compounds;Molecules;Spectroscopy;Quartz |
Issue Date: | 10-Apr-2004 |
Source: | Journal of physical chemistry B, 2004, vol. 108, no. 18, pp. 5489-5491 |
Volume: | 108 |
Issue: | 18 |
Start page: | 5489 |
End page: | 5491 |
Journal: | Journal of Physical Chemistry B |
Abstract: | Resonance Raman (RR) spectra are reported for the fully reduced carbon monoxy derivative of ba3-cytochrome c oxidase from Thermus thermophilus. The RR spectra show the formation of a photolabile six-coordinate heme-CO and a photostable five-coordinate heme Fe-CO species. The latter species is formed by the cleavage of the proximal heme Fe-His384 bond and is the first five-coordinate Fe-CO species detected in heme-copper oxidases. The frequency of the Fe-CO species observed at 526 cm-1 correlates with either the C-O stretching modes observed at 1967 or 1982 cm-1 and lie on the correlation line of v(Fe-CO) vs v(C-O) for all known five-coordinate heme Fe-CO complexes. The loss of intensity of the heme Fe-His384 mode observed at 193 cm-1 in the photostationary CO-bound spectra is attributed to the loss of the non-hydrogen bonded heme Fe-His384⋯Gly359 conformer. Taken together, the data indicate that the environment of the ruptured His384 that is a part of the Q-proton pathway and leads to the highly conserved among all heme-copper oxidases, H2O pool, is disrupted upon CO binding to heme a3 |
URI: | https://hdl.handle.net/20.500.14279/1921 |
ISSN: | 15206106 |
DOI: | 10.1021/jp049259k |
Rights: | © American Chemical Society Attribution-NonCommercial-NoDerivs 3.0 United States |
Type: | Article |
Affiliation: | University of Crete |
Affiliation : | University of Cyprus |
Publication Type: | Peer Reviewed |
Appears in Collections: | Άρθρα/Articles |
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