期刊
BIOCHEMISTRY
卷 46, 期 11, 页码 3423-3434出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi061854k
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资金
- NHLBI NIH HHS [R01 HL061411, R01 HL070755, R01 HL070755-08, HL 61411, HL 70755] Funding Source: Medline
- NIAID NIH HHS [U19 AI068021, U19 AI 068021] Funding Source: Medline
- NIOSH CDC HHS [OH 008282, R01 OH008282] Funding Source: Medline
Upon interaction with anionic phospholipids, particularly mitochondria-specific cardiolipin (CL), cytochrome c (cyt c) loses its tertiary structure and its peroxidase activity dramatically increases. CL-induced peroxidase activity of cyt c has been found to be important for selective CL oxidation in cells undergoing programmed death. During apoptosis, the peroxidase activity and the fraction of CL-bound cyt c markedly increase, suggesting that CL may act as a switch to regulate cyt c's mitochondrial functions. Using cyclic voltammetry and equilibrium redox titrations, we show that the redox potential of cyt c shifts negatively by 350-400 mV upon binding to CL-containing membranes. Consequently, functions of cyt c as an electron transporter and cyt c reduction by Complex III are strongly inhibited. Further, CL/cyt c complexes are not effective in scavenging superoxide anions and are not effectively reduced by ascorbate. Thus, both redox properties and functions of cyt c change upon interaction with CL in the mitochondrial membrane, diminishing cyt c's electron donor/acceptor role and stimulating its peroxidase activity.
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