Comparison Between O and OH Intermediates of Cytochrome c Oxidase Studied by FTIR Spectroscopy

Show full item record



Permalink

http://hdl.handle.net/10138/316050

Citation

Gorbikova , E & Kalendar , R 2020 , ' Comparison Between O and OH Intermediates of Cytochrome c Oxidase Studied by FTIR Spectroscopy ' , Frontiers in Chemistry , vol. 8 , 387 . https://doi.org/10.3389/fchem.2020.00387

Title: Comparison Between O and OH Intermediates of Cytochrome c Oxidase Studied by FTIR Spectroscopy
Author: Gorbikova, Elena; Kalendar, Ruslan
Contributor organization: Institute of Biotechnology
Department of Agricultural Sciences
Date: 2020-05-05
Language: eng
Number of pages: 6
Belongs to series: Frontiers in Chemistry
ISSN: 2296-2646
DOI: https://doi.org/10.3389/fchem.2020.00387
URI: http://hdl.handle.net/10138/316050
Abstract: Cytochrome c oxidase is terminal enzyme in the respiratory chain of mitochondria and many aerobic bacteria. It catalyzes reduction of oxygen to water. During its catalysis, CcO proceeds through several quite stable intermediates (R, A, PR/M, O/OH, E/EH). This work is concentrated on the elucidation of the differences between structures of oxidized intermediates O and OH in different CcO variants and at different pH values. Oxidized intermediates of wild type and mutated CcO from Paracoccus denitrificans were studied by means of static and time-resolved Fourier-transform infrared spectroscopy in acidic and alkaline conditions in the infrared region 1800–1000 cm−1. No reasonable differences were found between all variants in these conditions, and in this spectral region. This finding means that the binuclear center of oxygen reduction keeps a very similar structure and holds the same ligands in the studied conditions. The further investigation in search of differences should be performed in the 4000–2000 cm−1 IR region where water ligands absorb.
Subject: cell respiration
cytochrome c oxidase
oxidized state
FTIR spectroscopy
oxidoreduction
STRUCTURAL-CHANGES
CATALYTIC CYCLE
PROTON PUMP
RESOLUTION
REDUCTION
TRANSLOCATION
FORMS
STATE
STEP
1182 Biochemistry, cell and molecular biology
Peer reviewed: Yes
Rights: cc_by
Usage restriction: openAccess
Self-archived version: publishedVersion


Files in this item

Total number of downloads: Loading...

Files Size Format View
fchem_08_00387.pdf 1.354Mb PDF View/Open

This item appears in the following Collection(s)

Show full item record