Exploring Oxidation State Dependent Conformational Changes of Cytochrome C on Cardiolipin Containing Liposomes

Milorey, Bridget; Serpas, Lee; Pandiscia, Leah; Schweitzer‐Stenner, Reinhard

doi:10.1016/j.bpj.2015.11.2280

Biophysical Journal

2016

DOI: 10.1016/j.bpj.2015.11.2280

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Exploring Oxidation State Dependent Conformational Changes of Cytochrome C on Cardiolipin Containing Liposomes

Bridget Milorey

Lee Serpas

Leah Pandiscia

et al.

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“…The appearance of peroxidase activity in Cyt c has been attributed to the partial unfolding of the protein, ,, consequent rupture of the bond between the heme iron and its axial ligand Met80, ,− and formation of alternative non-native conformers. It is notable that such non-native conformers appear also to be able to induce reversible pore formation allowing translocation of Cyt c more readily across the inner mitochondrial membrane .…”

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Unravelling the Non-Native Low-Spin State of the Cytochrome c–Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only

et al. 2017

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The interaction between cytochrome c (Cyt c) and cardiolipin (CL) plays a vital role in the early stages of apoptosis. The binding of CL to Cyt c induces a considerable increase in its peroxidase activity that has been attributed to the partial unfolding of the protein, dissociation of the Met80 axial ligand, and formation of non-native conformers. Although the interaction between Cyt c and CL has been extensively studied, there is still no consensus regarding the conformational rearrangements of Cyt c that follow the protein-lipid interaction. To rationalize the different results and gain better insight into the Cyt c-CL interaction, we have studied the formation of the CL complex of the horse heart wild-type protein and selected mutants in which residues considered to play a key role in the interaction with CL (His26, His33, Lys72, Lys73, and Lys79) have been mutated. The analysis was conducted at both room temperature and low temperatures via ultraviolet-visible absorption, resonance Raman, and electron paramagnetic resonance spectroscopies. The trigger and the sequence of CL-induced structural variations are discussed in terms of disruption of the His26-Pro44 hydrogen bond. We unequivocally identify the sixth ligand in the partially unfolded, non-native low-spin state that Cyt c can adopt following the protein-lipid interaction, as a His ligation, ruling out the previously proposed involvement of a Lys residue or an OH ion.

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confidence: 99%

Unravelling the Non-Native Low-Spin State of the Cytochrome c–Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only

et al. 2017

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Exploring Oxidation State Dependent Conformational Changes of Cytochrome C on Cardiolipin Containing Liposomes

Cited by 1 publication

References 0 publications

Unravelling the Non-Native Low-Spin State of the Cytochrome c–Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only

Unravelling the Non-Native Low-Spin State of the Cytochrome c–Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only

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