Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen

Verfasser / Beitragende:
[Antonio Ranieri, Diego Millo, Giulia Di Rocco, Gianantonio Battistuzzi, Carlo Bortolotti, Marco Borsari, Marco Sola]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/3(2015-04-01), 531-540
Format:
Artikel (online)
ID: 605507384
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024 7 0 |a 10.1007/s00775-015-1238-6  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00775-015-1238-6 
245 0 0 |a Immobilized cytochrome c bound to cardiolipin exhibits peculiar oxidation state-dependent axial heme ligation and catalytically reduces dioxygen  |h [Elektronische Daten]  |c [Antonio Ranieri, Diego Millo, Giulia Di Rocco, Gianantonio Battistuzzi, Carlo Bortolotti, Marco Borsari, Marco Sola] 
520 3 |a Mitochondrial cytochrome c (cytc) plays an important role in programmed cell death upon binding to cardiolipin (CL), a negatively charged phospholipid of the inner mitochondrial membrane (IMM). Although this binding has been thoroughly investigated in solution, little is known on the nature and reactivity of the adduct (cytc-CL) immobilized at IMM. In this work, we have studied electrochemically cytc-CL immobilized on a hydrophobic self-assembled monolayer (SAM) of decane-1-thiol. This construct would reproduce the motional restriction and the nonpolar environment experienced by cytc-CL at IMM. Surface-enhanced resonance Raman (SERR) studies allowed the axial heme iron ligands to be identified, which were found to be oxidation state dependent and differ from those of cytc-CL in solution. In particular, immobilized cytc-CL experiences an equilibrium between a low-spin (LS) 6c His/His and a high-spin (HS) 5c His/− coordination states. The former prevails in the oxidized and the latter in the reduced form. Axial coordination of the ferric heme thus differs from the (LS) 6c His/Lys and (LS) 6c His/OH− states observed in solution. Moreover, a relevant finding is that the immobilized ferrous cytc-CL is able to catalytically reduce dioxygen, likely to superoxide ion. These findings indicate that restriction of motional freedom due to interaction with the membrane is an additional factor playing in the mechanism of cytc unfolding and cytc-mediated peroxidation functional to the apoptosis cascade. 
540 |a SBIC, 2015 
690 7 |a Cytochrome c  |2 nationallicence 
690 7 |a Cardiolipin  |2 nationallicence 
690 7 |a Electrochemistry  |2 nationallicence 
690 7 |a SERRS  |2 nationallicence 
690 7 |a Apoptosis  |2 nationallicence 
690 7 |a Dioxygen interaction  |2 nationallicence 
690 7 |a cytc : Cytochrome c  |2 nationallicence 
690 7 |a ycc : Recombinant untrimethylated Saccharomyces cerevisiae yeastiso-1-cytochrome c  |2 nationallicence 
690 7 |a KtoA : Recombinant untrimethylated Saccharomyces cerevisiae yeastiso-1-cytochrome c variant K72A/K73A/K79A  |2 nationallicence 
690 7 |a CL : Cardiolipin  |2 nationallicence 
700 1 |a Ranieri  |D Antonio  |u Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125, Modena, Italy  |4 aut 
700 1 |a Millo  |D Diego  |u Department of Physics and Astronomy, LaserLaB Amsterdam, Vrije Universiteit, De Boelelaan 1083, 1081 HV, Amsterdam, The Netherlands  |4 aut 
700 1 |a Di Rocco  |D Giulia  |u Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125, Modena, Italy  |4 aut 
700 1 |a Battistuzzi  |D Gianantonio  |u Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, via Campi 183, 41125, Modena, Italy  |4 aut 
700 1 |a Bortolotti  |D Carlo  |u Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125, Modena, Italy  |4 aut 
700 1 |a Borsari  |D Marco  |u Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, via Campi 183, 41125, Modena, Italy  |4 aut 
700 1 |a Sola  |D Marco  |u Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125, Modena, Italy  |4 aut 
773 0 |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/3(2015-04-01), 531-540  |x 0949-8257  |q 20:3<531  |1 2015  |2 20  |o 775 
856 4 0 |u https://doi.org/10.1007/s00775-015-1238-6  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00775-015-1238-6  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Ranieri  |D Antonio  |u Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125, Modena, Italy  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Millo  |D Diego  |u Department of Physics and Astronomy, LaserLaB Amsterdam, Vrije Universiteit, De Boelelaan 1083, 1081 HV, Amsterdam, The Netherlands  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Di Rocco  |D Giulia  |u Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125, Modena, Italy  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Battistuzzi  |D Gianantonio  |u Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, via Campi 183, 41125, Modena, Italy  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Bortolotti  |D Carlo  |u Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125, Modena, Italy  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Borsari  |D Marco  |u Department of Chemical and Geological Sciences, University of Modena and Reggio Emilia, via Campi 183, 41125, Modena, Italy  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Sola  |D Marco  |u Department of Life Sciences, University of Modena and Reggio Emilia, Via Campi 183, 41125, Modena, Italy  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/3(2015-04-01), 531-540  |x 0949-8257  |q 20:3<531  |1 2015  |2 20  |o 775