Low-temperature electron paramagnetic resonance study of the ferricytochrome c-cardiolipin complex

Vincent, James S.; Kon, Hideo; Levin, Ira W.

doi:10.1021/bi00382a036

Cited by 35 publications

(22 citation statements)

References 16 publications

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“…These findings indicate that also cyt3+-AOT exhibits a mixture of the conformational states I and 11. Thus, the present study also provides the key for the understanding of the drastic changes in the C D and absorption spectra of cyt3+ c in AOT micelles [see, for example, Douzou et al (1979), Pileni (1981) In this context it is interesting to refer to a recent EPR study on the cyt'+-cardiolipin complex by Vincent et al (1987), who concluded that the structure of the 6cLS form of the bomd cytg+ c is modified and in addition a weak contribution of HS signals (15%) was detected. FIGURE 7: Difference spectrum of the RR spectra of cyt' +-PV complex and the dissolved cytf: (413-nm excitation).…”

Section: Resultsmentioning

confidence: 80%

Cytochrome c at charged interfaces. 2. Complexes with negatively charged macromolecular systems studied by resonance Raman spectroscopy

Hildebrandt

Stockburger

1989

Biochemistry

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We have analyzed the structure of cytochrome c (cyt c) bound in a variety of complexes in which negatively charged molecular groups interact with the positively charged binding domain around the heme crevice of cyt c. Using resonance Raman spectroscopy, we could demonstrate that these interactions induce the same conformational changes as they were observed in the surface-enhanced resonance Raman experiments of cyt c adsorbed on the Ag electrode [Hildebrandt & Stockburger (1989) Biochemistry (preceding paper in this issue)]. When cyt c is bound to (As4W400140)27-, state I1 is stabilized, whereas in complexes with phosvitin and cytochrome b5 state I is formed. The complexes with phospholipid vesicles and inverted micelles reveal a mixture of both states. It is suggested that these systems as well as cyt c adsorbed on the Ag electrode may be regarded as model systems for the physiological complexes of cyt c with cytochrome oxidase and cytochrome reductase. On the basis of our findings it is proposed that the biological electron-transfer reactions are controlled by electric field induced conformational transitions of cyt c upon complex formation with its physiological redox partners.

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Section: Resultsmentioning

confidence: 80%

Cytochrome c at charged interfaces. 2. Complexes with negatively charged macromolecular systems studied by resonance Raman spectroscopy

Hildebrandt

Stockburger

1989

Biochemistry

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“…(iii) Unlike in PC/PE/CL vesicles, the EPR spectra in DCP vesicles clearly show the presence of both spin states (low and high). The existence of this high spin state species has been described in the literature as a denatured cytochrome c (23). However, the addition of NaCl promotes the detachment of the hemeprotein from the membrane as observed by the decrease of the signal of the high spin state form and the recuperation of the signal of the native low spin state form (not shown).…”

Section: The Association Of Ferric and Ferrous Cytochrome C With Charmentioning

confidence: 72%

Effect of Heme Iron Valence State on the Conformation of Cytochrome c and Its Association with Membrane Interfaces

Nantes

Zucchi

Nascimento

et al. 2001

Journal of Biological Chemistry

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Recently cytochrome c has been mentioned as an important mediator in the events of cellular oxidative stress and apoptosis. To investigate the influence of charged interfaces on the conformation of cytochrome c, the CD and magnetic circular dichroic behavior of ferric and ferrous cytochrome c in homogeneous medium and in phosphatidylcholine/phosphatidylethanolamine/cardiolipin and dicetylphosphate liposomes was studied in the 300 -600 and 200 -320 nm wavelength region. EPR spectra demonstrate that the association of cytochrome c with membranes promotes alterations of the crystal field symmetry and spin state of the heme Fe 3؉ . The studies also include the effect of P i , NaCl, and CaCl 2 . Magnetic circular dichroism and CD results show that the interaction of both ferrous and ferric cytochrome c with charged interfaces promotes conformational changes in the ␣-helix content, tertiary structure, and heme iron spin state. Moreover, the association of cytochrome c with different liposomes is sensitive to the heme iron valence state. The more effective association with membranes occurs with ferrous cytochrome c. Dicetylphosphate liposomes, as a negatively charged membrane model, promoted a more pronounced conformational modification in the cytochrome c structure. A decrease in the lipid/protein association is detected in the presence of increasing amounts of CaCl 2 , NaCl, and P i , in response to the increase of the ionic strength.

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“…Cardiolipin interaction with the C-site results in a tightly bound configuration, in which one cardiolipin acyl chain is inserted into the hydrophobic groove while keeping the other chains embedded within the mitochondrial inner membrane (Tuominen et al, 2002). This interaction essentially tethers Cyt c to the membrane and gives rise to the extended lipid anchorage hypothesis that is supported by mounting evidence of heme-iron spectral changes (Choi and Swanson, 1995; Spooner and Watts, 1991; Tuominen et al, 2002; Vincent et al, 1987; Vincent and Levin, 1988). An alternative hypothesis suggesting interactions of two fatty acyls of cardiolipin with Cyt c has also been suggested (Sinibaldi et al, 2010).…”

Section: Role Of Cytochrome C In Apoptosismentioning

confidence: 90%

The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis

et al. 2011

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Cytochrome c (Cytc) is essential in mitochondrial electron transport and intrinsic type II apoptosis. Mammalian Cytc also scavenges reactive oxygen species (ROS) under healthy conditions, produces ROS with the co-factor p66 Shc , and oxidizes cardiolipin during apoptosis. The recent finding that Cytc is phosphorylated in vivo underpins a model for the pivotal role of Cytc regulation in making life and death decisions. An apoptotic sequence of events is proposed involving changes in Cytc phosphorylation, increased ROS via increased mitochondrial membrane potentials or the p66 Shc pathway, the oxidation of cardiolipin by Cytc, and its release from the mitochondria. Cytc regulation in respiration and cell death is discussed in a human disease context including neurodegenerative and cardiovascular diseases, cancer, and sepsis.

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Low-temperature electron paramagnetic resonance study of the ferricytochrome c-cardiolipin complex

Cited by 35 publications

References 16 publications

Cytochrome c at charged interfaces. 2. Complexes with negatively charged macromolecular systems studied by resonance Raman spectroscopy

Cytochrome c at charged interfaces. 2. Complexes with negatively charged macromolecular systems studied by resonance Raman spectroscopy

Effect of Heme Iron Valence State on the Conformation of Cytochrome c and Its Association with Membrane Interfaces

The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: From respiration to apoptosis

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