Molecular mechanisms for the induction of peroxidase activity of the cytochrome c–cardiolipin complex

Abe, Masato; Tanabe, Yukie; Kosaka, Atsuko; Miki, Yuko; Miyoshi, Hideto

doi:10.1016/j.bbabio.2014.05.290

Cited by 19 publications

(50 citation statements)

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“…4 Recently, several studies have found that the interaction of cyt c with cardiolipin (CL), a negatively charged mitochondrial phospholipid bearing four fatty acyl chains, promotes partial unfolding of the protein and dissociation of the Met80 ligand from the heme. 8 In order to reveal the apoptosis mechanism induced by the cyt c-CL complex, some advanced techniques and strategies have been applied to investigate the complex from different perspectives. 7 Induction of the 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 peroxidase activity of cyt c by CL and H 2 O 2 in mitochondria is suggested to be a key event in early apoptosis.…”

Section: Introductionmentioning

confidence: 99%

Label-Free Surface-Enhanced Infrared Spectroelectrochemistry Studies the Interaction of Cytochrome c with Cardiolipin-Containing Membranes

Liu

Zeng

et al. 2015

J. Phys. Chem. C

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Interactions of cytochrome c (cyt c) with cardiolipin (CL)-containing membranes have been revealed to play an important role in inducing early apoptosis. In this paper, we studied the interaction of cyt c with solid-supported CL-containing lipid bilayers by a lable-free spectroelectrochemistry method. The biomimetic membrane was fabricated by fusing cardiolipin-phosphatidylcholine (CL_PC, 1:4) vesicles onto the hydrophobic surface of a preadsorbed 1-dodecanethiol (DT) on a gold electrode (CL_PC/DT/Au). The adsorption of cyt c onto the CL_PC/DT/Au was in-situ studied by cyclic voltammetry (CV) and surface-enhanced Infrared adsorption spectroscopy (SEIRAS). The electrochemistry of Cyt c/CL_PC/DT/Au exhibits the formal potential (E f ) at 0.21 V (vs. Ag/AgCl), a positive shift of 190 mV as compared to that of native cyt c adsorbed at the mercaptoundecanoic acid-modified gold Page 1 of 34 ACS Paragon Plus Environment The Journal of Physical Chemistry 2 electrode (Cyt c/MUA/Au). The potential-induced SEIRA difference spectroscopy discloses that cyt c was loosely adsorbed onto CL_PC/DT/Au in a different orientation, and underwent a new β-sheet formation relative to native cyt c adsorbed onto MUA/Au. It could be the enhanced hydration change of CL-bound cyt c upon oxidization and reduction and the different adsorption orientation that determine the positive shift in its formal potential.

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Section: Introductionmentioning

confidence: 99%

Label-Free Surface-Enhanced Infrared Spectroelectrochemistry Studies the Interaction of Cytochrome c with Cardiolipin-Containing Membranes

Liu

Zeng

et al. 2015

J. Phys. Chem. C

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“…An initial step in this process involves changes in the cyt c-CL interaction that anchors the protein to the inner membrane. Attendant protein conformational changes and hydrophobic interactions with the lipid confer catalytic activities to the cyt c-CL complex (1,4,(9)(10)(11)(12), which causes CL oxidation. Signaling at this stage may also involve cyt c tyrosine phosphorylation (13,14) and the balance of mitochondrial ATP (15).…”

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confidence: 99%

Cytochrome c causes pore formation in cardiolipin-containing membranes

Bergstrom

Beales

Yang

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

127

135

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The release of cytochrome c from mitochondria is a key signaling mechanism in apoptosis. Although extramitochondrial proteins are thought to initiate this release, the exact mechanisms remain unclear. Cytochrome c (cyt c) binds to and penetrates lipid structures containing the inner mitochondrial membrane lipid cardiolipin (CL), leading to protein conformational changes and increased peroxidase activity. We describe here a direct visualization of a fluorescent cyt c crossing synthetic, CL-containing membranes in the absence of other proteins. We observed strong binding of cyt c to CL in phospholipid vesicles and bursts of cyt c leakage across the membrane. Passive fluorescent markers such as carboxyfluorescein and a 10-kDa dextran polymer crossed the membrane simultaneously with cyt c, although larger dextrans did not. The data show that these bursts result from the opening of lipid pores formed by the cyt c-CL conjugate. Pore formation and cyt c leakage were significantly reduced in the presence of ATP. We suggest a model, consistent with these findings, in which the formation of toroidal lipid pores is driven by initial cyt c-induced negative spontaneous membrane curvature and subsequent protein unfolding interactions. Our results suggest that the CL-cyt c interaction may be sufficient to allow cyt c permeation of mitochondrial membranes and that cyt c may contribute to its own escape from mitochondria during apoptosis.

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“…Cyt c cannot function as a peroxidase until modified, because it is a hexacoordinate heme protein and has not a free coordination site for substrate binding [36,37]. For example, it was demonstrated that partial unfolding [51], oxidation [36], and structural perturbations induced by a mutation [37] increased the peroxidase-like activity of cyt c by facilitating the access of H 2 O 2 and other substrates to the catalytic site. It has been pointed out that cyt c may be a catalyst of H 2 DCF oxidation [31].…”

Section: Discussionmentioning

confidence: 97%