Structural changes and picosecond to second dynamics of cytochrome c in interaction with nitric oxide in ferrous and ferric redox states

Kruglik, Sergei G.; Yoo, Byung‐Kuk; Lambry, Jean−Christophe; Martin, Jean−Louis; Négrerie, Michel

doi:10.1039/c7cp02634j

Cited by 15 publications

(14 citation statements)

References 81 publications

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“…On the other hand, nitrosylation of Cc induces changes in protein conformation and heme configuration/coordination [89]. Such effects on redox Cc properties inhibit its peroxidase activity and enhance its ability to activate the caspase cascade.…”

Section: Nitration and Nitrosylationmentioning

confidence: 99%

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Post-Translational Modifications of Cytochrome c in Cell Life and Disease

Guerra‐Castellano

Márquez

Pérez‐Mejías

et al. 2020

IJMS

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Mitochondria are the powerhouses of the cell, whilst their malfunction is related to several human pathologies, including neurodegenerative diseases, cardiovascular diseases, and various types of cancer. In mitochondrial metabolism, cytochrome c is a small soluble heme protein that acts as an essential redox carrier in the respiratory electron transport chain. However, cytochrome c is likewise an essential protein in the cytoplasm acting as an activator of programmed cell death. Such a dual role of cytochrome c in cell life and death is indeed fine-regulated by a wide variety of protein post-translational modifications. In this work, we show how these modifications can alter cytochrome c structure and functionality, thus emerging as a control mechanism of cell metabolism but also as a key element in development and prevention of pathologies.

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Section: Nitration and Nitrosylationmentioning

confidence: 99%

“…Such effects on redox Cc properties inhibit its peroxidase activity and enhance its ability to activate the caspase cascade. For this reason, it has been proposed that Cc nitrosylation is a proapoptotic modification [88,89,124].…”

Section: Nitration and Nitrosylationmentioning

confidence: 99%

Post-Translational Modifications of Cytochrome c in Cell Life and Disease

Guerra‐Castellano

Márquez

Pérez‐Mejías

et al. 2020

IJMS

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“…The prominent mode around 1370 cm –1 can be assigned to ν 4 of the symmetrical stretch mode of a pyrrole half-ring in the heme structure. ,− ,− The probe delay dependence of this mode was calculated from the spectrograms in Figure a,b and plotted in Figure a,b.…”

Section: Resultsmentioning

confidence: 99%

“…Vibrational Dynamics Observed in TA Signal. Timeresolved Raman or infrared (IR) spectroscopy 24,25 can study the vibrational spectroscopic dynamics for Raman active and IR active vibration modes, respectively, to study their growth and relaxation lifetimes reflecting the transition to the intermediate state; however, they are hard to be applied to the study of the transient state by continuously changing their mode frequencies. In the present work, we have performed TA spectroscopy by exciting the samples by a sub-10 fs pulse, which produces a wavepacket in the electronic state oscillating on the potential energy surface at the period of molecular vibration.…”

Section: ■ Introductionmentioning

confidence: 99%

“…However, TA spectroscopy does not provide the information sensitive to the molecular structure change and is hard to support the assignment of Fe–Met80 dissociation and recombination. TA spectroscopy was followed by time-resolved resonance Raman (TR 3 ) spectroscopy, ,− broadband impulsive vibrational spectroscopy (BB-IVS), impulsive stimulated Raman scattering (ISRS), − and femtosecond stimulated resonance Raman spectroscopy (FSRRS), − which can study the molecular vibration frequency change reflecting the molecular structure change during the reaction and provide direct information about the transient structure evolution of heme.…”

Section: Introductionmentioning

confidence: 99%

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Primary Electronic and Vibrational Dynamics of Cytochrome c Observed by Sub-10 fs NUV Laser Pulses

Yabushita

Kobayashi

2020

J. Phys. Chem. B

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The primary reaction mechanism of cytochrome c (Cyt c) was elucidated for two redox forms of ferric (oxidized) and ferrous (reduced) Cyt c by measuring their transient absorption (TA) spectra using a homemade sub-10 fs broadband NUV laser pulses system. The TA traces measured in the broad probe wavelength region were analyzed by the global analysis method to study the electronic dynamics. The difference of relaxation dynamics dependent on the excitation bandwidth enabled us to elucidate that the 2.5 ps component in ferrous Cyt c can be assigned to intramolecular vibration energy redistribution and not to vibrational cooling, which was not clear until this work. The temporal resolution of 10 fs observes TA signal modulation caused by the molecular vibration in the time domain, which can be used to calculate the instantaneous frequency of the molecular vibration mode. The observed vibrational dynamics has visualized that the heme structure changes in 0.8 ps for ferric Cyt c and in >1.0 ps for ferrous Cyt c. These estimated lifetimes of vibrational dynamics reflect vibrational relaxation in the ground state of ferric Cyt c and electronic transition from the S2 state to the S1 state in ferrous Cyt c, respectively.

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Label‐free tracking of cytochrome C oxidation state in live cells by resonance Raman imaging

Szczesny‐Malysiak,

Bartkowiak,

Dybas

2024

FEBS Letters

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Free interconversion of cytochrome C (CytC) between native ferrous (Cyt‐FeII) and oxidized ferric (CytC‐FeIII) states is necessary to maintain the respiratory function of mitochondria. Disturbances in CytC‐FeIII to total CytC ratio may indicate mitochondrial dysfunction and apoptosis. Thus, tracking CytC oxidation state delivers important information about cellular physiology. In this work, we propose a novel methodology based on resonance Raman (rR) imaging optimized uniquely to track and qualitatively analyze the transition of Cyt‐FeII to CytC‐FeIII within live cells without affecting their morphology. None of the commonly used excitation lines allows such clear‐cut differentiation, contrary to the 405 nm applied in this work. The presented methodology provides a novel pathway in the label‐free detection of ferrous and ferric heme proteins.

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Structural changes and picosecond to second dynamics of cytochrome c in interaction with nitric oxide in ferrous and ferric redox states

Abstract: Negrerie. Structural changes and picosecond to second dynamics of cytochrome c in interaction with nitric oxide in ferrous and ferric redox states. Physical Chemistry Chemical Physics, Royal Society of Chemistry, 2017, 19 (32)

Cited by 15 publications

References 81 publications

Post-Translational Modifications of Cytochrome c in Cell Life and Disease

Post-Translational Modifications of Cytochrome c in Cell Life and Disease

Primary Electronic and Vibrational Dynamics of Cytochrome c Observed by Sub-10 fs NUV Laser Pulses

Label‐free tracking of cytochrome C oxidation state in live cells by resonance Raman imaging

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