scholarly journals Comparison between O and OH intermediates of cytochrome c oxidase studied by FTIR spectroscopy

2018 ◽  
Author(s):  
E. Gorbikova ◽  
R. Kalendar
Keyword(s):  
Fourier Transform ◽  
Paracoccus Denitrificans ◽  
Fourier Transform Infrared ◽  
Infrared Region ◽  
Wild Type ◽  
Hydrogen Electrode ◽  
Time Resolved ◽  
Alkaline Conditions ◽  
Binuclear Center ◽  
Water Ligands

AbstractCytochrome 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.AbbreviationsAferrous-oxy intermediateATRAttenuated total reflectanceBGbackgroundBNCbinuclear centerCcOCytochrome c oxidaseEone-electron reduced intermediateFferryl intermediateFRCOfully-reduced CO-inhibited enzymeFTIRFourier transform infraredIRinfraredNHENormal Hydrogen ElectrodeN-sidenegatively charged side of the membranePR/M“peroxy”intermediates; P-sidepositively charged side of the membraneRfully-reduced intermediateTRtime-resolvedWTwild type

scholarly journals Probing the Proton-Loading Site of Cytochrome C Oxidase Using Time-Resolved Fourier Transform Infrared Spectroscopy

Molecules ◽  
2020 ◽  
Vol 25 (15) ◽  
pp. 3393
Author(s):  
Elena Gorbikova ◽  
Sergey A. Samsonov ◽  
Ruslan Kalendar
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Fourier Transform Infrared Spectroscopy ◽  
Paracoccus Denitrificans ◽  
Fourier Transform Infrared ◽  
Double Difference ◽  
Time Resolved ◽  
Fast Kinetic

Crystal structure analyses at atomic resolution and FTIR spectroscopic studies of cytochrome c oxidase have yet not revealed protonation or deprotonation of key sites of proton transfer in a time-resolved mode. Here, a sensitive technique to detect protolytic transitions is employed. In this work, probing a proton-loading site of cytochrome c oxidase from Paracoccus denitrificans with time-resolved Fourier transform infrared spectroscopy is presented for the first time. For this purpose, variants with single-site mutations of N131V, D124N, and E278Q, the key residues in the D-channel, were studied. The reaction of mutated CcO enzymes with oxygen was monitored and analyzed. Seven infrared bands in the “fast” kinetic spectra were found based on the following three requirements: (1) they are present in the “fast” phases of N131V and D124N mutants, (2) they have reciprocal counterparts in the “slow” kinetic spectra in these mutants, and (3) they are absent in “fast” kinetic spectra of the E278Q mutant. Moreover, the double-difference spectra between the first two mutants and E278Q revealed more IR bands that may belong to the proton-loading site protolytic transitions. From these results, it is assumed that several polar residues and/or water molecule cluster(s) share a proton as a proton-loading site. This site can be propionate itself (holding only a fraction of H+), His403, and/or water cluster(s).

Construction of a Multichannel Fourier Transform Infrared Spectrometer for Single-Event Time-Resolved Spectroscopy

1996 ◽  
Vol 50 (8) ◽  
pp. 1030-1033 ◽  
Author(s):  
Mamoru Hashimoto ◽  
Hiro-O Hamaguchi
Keyword(s):  
Fourier Transform ◽  
Phase Transitions ◽  
Fourier Transform Infrared ◽  
Infrared Region ◽  
Single Event ◽  
Time Resolved ◽  
Time Resolved Spectroscopy ◽  
Event Time ◽  
Fourier Transform Infrared Spectrometer ◽  
Infrared Spectrometer

A newly designed multichannel Fourier transform infrared spectrometer has been constructed for single-event time-resolved spectroscopy. It is capable of measuring unrepeatable transient events such as phase transitions, explosions, etc., with a time resolution of up to 5.14 ms. The mid-infrared region of 4500–2500 cm−1 is covered with a maximum spectral resolution of 13 cm−1. The developed system is used to measure the phase transitions of alkanes. The solid–solid and solid–liquid phase transitions of octadecane and nonadecane have been studied with time resolutions of 5–50 ms.

Dependence of the intrinsic phase structure of Bi2O3 catalysts on photocatalytic CO2 reduction

2021 ◽  
Vol 11 (6) ◽  
pp. 2021-2025
Author(s):  
Liujin Wei ◽  
Guan Huang ◽  
Yajun Zhang
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Fourier Transform Infrared Spectroscopy ◽  
Phase Structure ◽  
Co2 Reduction ◽  
Fourier Transform Infrared ◽  
Time Resolved ◽  
Dependent Activity

The combination of time-resolved transient photoluminescence with in-situ Fourier transform infrared spectroscopy has been conducted to investigate the intrinsic phase structure-dependent activity of Bi2O3 catalyst for CO2 reduction.

Complexation of Polyacrylates by Ca2+Ions. Time-Resolved Studies Using Attenuated Total Reflectance Fourier Transform Infrared Dialysis Spectroscopy

Langmuir ◽  
2004 ◽  
Vol 20 (7) ◽  
pp. 2539-2542 ◽  
Author(s):  
Fabiana Fantinel ◽  
Jens Rieger ◽  
Ferenc Molnar ◽  
Patrick Hübler
Keyword(s):  
Fourier Transform ◽  
Fourier Transform Infrared ◽  
Attenuated Total Reflectance ◽  
Time Resolved ◽  
Total Reflectance

Reaction Mechanism of Adenylyltransferase DrrA fromLegionella pneumophilaElucidated by Time-Resolved Fourier Transform Infrared Spectroscopy

2014 ◽  
Vol 136 (26) ◽  
pp. 9338-9345 ◽  
Author(s):  
Konstantin Gavriljuk ◽  
Jonas Schartner ◽  
Aymelt Itzen ◽  
Roger S. Goody ◽  
Klaus Gerwert ◽  
...  
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Reaction Mechanism ◽  
Fourier Transform Infrared Spectroscopy ◽  
Fourier Transform Infrared ◽  
Time Resolved

Time-resolved Fourier transform infrared emission spectroscopy of He2 produced by a pulsed discharge

2004 ◽  
Vol 383 (3-4) ◽  
pp. 256-260 ◽  
Author(s):  
Yukio Hosaki ◽  
Svatopluk Civiš ◽  
Kentarou Kawaguchi
Keyword(s):  
Fourier Transform ◽  
Emission Spectroscopy ◽  
Fourier Transform Infrared ◽  
Infrared Emission ◽  
Pulsed Discharge ◽  
Time Resolved ◽  
Infrared Emission Spectroscopy

Real-Time Pursuit of Crystal Growth by Millisecond Time-Resolved Multichannel Fourier Transform Infrared Spectroscopy

1998 ◽  
Vol 52 (2) ◽  
pp. 222-225
Author(s):  
Mamoru Hashimoto ◽  
Hiro-O Hamaguchi
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Structural Change ◽  
Liquid Phase ◽  
Fourier Transform Infrared Spectroscopy ◽  
Molecular Orientation ◽  
Structural Changes ◽  
Fourier Transform Infrared ◽  
Time Resolved ◽  
Recovery Curves

The surface (about 130 molecular layers) of an oriented thin crystal of decanoic acid was subjected to sudden melting by a laser-induced temperature jump (T-jump), and the process of subsequent crystal re-growth was monitored by millisecond time-resolved multichannel Fourier transform infrared spectroscopy. The gauche–trans structural change of the alkane part of the molecule has been probed by the CH stretch bands in the 2800–3000 cm−1 region. The change in the molecular orientation has been detected by the OH stretch band around 3065 cm−1. The recovery curves for the CH2 antisymmetric stretch and the OH stretch bands are markedly different from each other in the first 200 ms, suggesting that the gauche–trans structural changes precedes the crystal re-growth. After 500 ms, the recovery curves become identical. This result means that the rate of the gauche to the trans structural change is equal to the rate of the recovery of the molecular orientation. It is highly likely that a fast equilibrium is attained between the gauche and the trans conformations in the liquid phase after 500 ms from the sudden melting and that the crystal re-growth takes place solely via the all-trans structure in the liquid phase.

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