Results 1 to 10 of about 20,306,851 (378)

New insight into the mechanism of mitochondrial cytochrome c function. [PDF]

PLoS ONE, 2017
We investigate functional role of the P76GTKMIFA83 fragment of the primary structure of cytochrome c. Based on the data obtained by the analysis of informational structure (ANIS), we propose a model of functioning of cytochrome c. According to this model,
Rita V Chertkova, Nadezda A Brazhe, Tatiana V Bryantseva, Alexey N Nekrasov, Dmitry A Dolgikh, Alexander I Yusipovich, Olga Sosnovtseva, Georgy V Maksimov, Andrei B Rubin, Mikhail P Kirpichnikov   +9 more
doaj   +2 more sources

Oxidative stress is tightly regulated by cytochrome c phosphorylation and respirasome factors in mitochondria [PDF]

Proceedings of the National Academy of Sciences of the United States of America, 2018
Respiratory cytochrome c has been found to be phosphorylated at tyrosine 97 in the postischemic brain upon neuroprotective insulin treatment, but how such posttranslational modification affects mitochondrial metabolism is unclear.
Díaz Moreno, Irene, Díaz Quintana, Antonio Jesús, Elena-Real, Carlos A., García Mauriño, Sofía M., González Arzola, Katiuska, Guerra Castellano, Alejandra, Pérez Mejías, Gonzalo, Rosa Acosta, Miguel Ángel de la   +7 more
core   +2 more sources

Structural Insights into Mechanisms Underlying Mitochondrial and Bacterial Cytochrome c Synthases [PDF]

Biomolecules
Mitochondrial holocytochrome c synthase (HCCS) is an essential protein in assembling cytochrome c (cyt c) of the electron transport system. HCCS binds heme and covalently attaches the two vinyls of heme to two cysteine thiols of the cyt c CXXCH motif ...
Pema L. Childs, Ethan P. Lowder, Deanna L. Mendez, Shalon E. Babbitt, Amidala Martinie, Jonathan Q. Huynh, Robert G. Kranz   +6 more
doaj   +2 more sources

Import of cytochrome c into mitochondria [PDF]

European Journal of Biochemistry, 1987
The import of cytochrome c into mitochondria can be resolved into a number of discrete steps. Here we report on the covalent attachment of heme to apocytochrome c by the enzyme cytochrome c heme lyase in mitochondria from Neurospora crassa. A new method
Basile G., Burnette W. N., Chance B., Dumont M. E., Ernst V., Estabrook R. W., Freitag H., Gasser S. M., Hackenbrock C. R., Hay R., Heller J., Hennig B., Hennig B., Hennig B., Kanarek L., Korb H., Laemmli U. K., Lederer F., Matner R. R., Matsuura S., Means G. E., Mihara K., Nicholson D. W., Nozaki M., Pelham H. R. B., Rietveld A., Rietveld A., Rietveld A., Rietveld A., Scarpulla R. C., Schmidt B., Sherman F., Stewart J. W., Taniuchi H., Taniuchi H., Towbin H., Veloso D., Visco C., Yuan P.-M., Zimmermann R., Zimmermann R., Zimmermann R., Zitomer R. S.   +42 more
core   +5 more sources

Cytochrome c signalosome in mitochondria [PDF]

European Biophysics Journal, 2011
Cytochrome c delicately tilts the balance between cell life (respiration) and cell death (apoptosis). Whereas cell life is governed by transient electron transfer interactions of cytochrome c inside the mitochondria, the cytoplasmic adducts of cytochrome
Díaz Moreno, Irene, Díaz Quintana, Antonio Jesús, García Heredia, José Manuel, Rosa Acosta, Miguel Ángel de la   +3 more
core   +7 more sources

Complexation of CcmB with CcmACD safeguards heme translocation for cytochrome c maturation [PDF]

mLife
Cytochrome c maturation (CCM), a posttranslational modification involving covalent attachment of heme to polypeptides (apocyt c), is essential for the activity and cellular function of cytochromes c.
Yuanyou Xu, Wei Wang, Qianrou Zhang, Sirui Han, Jiahao Wang, Shihua Wu, Haichun Gao   +6 more
doaj   +2 more sources

Release of Cytochrome C from Bax Pores at the Mitochondrial Membrane

Scientific Reports, 2017
How cytochrome C is released from the mitochondria to the cytosol via Bax oligomeric pores, a process which is required for apoptosis, is still a mystery.
Mingzhen Zhang, Jie Zheng, Ruth Nussinov, Buyong Ma   +3 more
doaj   +2 more sources

Biochemical mapping reveals a conserved heme transport mechanism via CcmCD in System I bacterial cytochrome c biogenesis [PDF]

mBio
Heme is a redox-active cofactor for essential processes across all domains of life. Heme’s redox capabilities are responsible for its biological significance but also make it highly cytotoxic, requiring tight intracellular regulation.
Alicia N. Kreiman, Sarah E. Garner, Susan C. Carroll, Molly C. Sutherland   +3 more
doaj   +2 more sources

THE CYTOCHROME c-AZIDE COMPLEX

Journal of Biological Chemistry, 1948
B.L. Horecker, J. N. Stannard
openalex   +6 more sources

Cytochrome c Negatively Regulates NLRP3 Inflammasomes. [PDF]

PLoS ONE, 2016
The release of cytochrome c from the inner mitochondrial membrane, where it is anchored by caridolipin, triggers the formation of the Apaf-1 apoptosome. Cardiolipin also interacts with NLRP3 recruiting NLRP3 to mitochondria and facilitating inflammasome ...
Chong-Shan Shi, John H Kehrl
doaj   +1 more source