scholarly journals The alkaline transition of cytochrome c revisited: Effects of electrostatic interactions and tyrosine nitration on the reaction dynamics

2019 ◽  
Vol 665 ◽  
pp. 96-106 ◽  
Author(s):  
Santiago Oviedo-Rouco ◽  
María A. Castro ◽  
Damián Alvarez-Paggi ◽  
Cecilia Spedalieri ◽  
Verónica Tortora ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Electrostatic Interactions ◽  
Reaction Dynamics ◽  
Tyrosine Nitration ◽  
Alkaline Transition

scholarly journals Structural and functional changes induced by tyrosine nitration in cytochrome c, a bi-functional protein

2010 ◽  
Vol 1797 ◽  
pp. 70
Author(s):  
Miguel A. De la Rosa ◽  
José M. García-Heredia ◽  
Jonathan Martínez-Fábregas ◽  
Pedro M. Nieto ◽  
Silvia Rubio-Novella ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Tyrosine Nitration ◽  
Functional Protein ◽  
Functional Changes

Monitoring alkaline transitions of yeast iso-1 cytochrome c at natural isotopic abundance using trimethyllysine as a native NMR probe

2018 ◽  
Vol 54 (89) ◽  
pp. 12630-12633 ◽  
Author(s):  
Peng Sun ◽  
Qianwen Wang ◽  
Bin Yuan ◽  
Qinjun Zhu ◽  
Bin Jiang ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Isotopic Abundance ◽  
Natural Isotopic Abundance ◽  
Alkaline Transition

A solution 1H–14N HSQC experiment has been employed to monitor the alkaline transition of yeast iso-1 cytochrome c.

Involvement of electrostatic interactions in cytochrome c complex formations

Biochimie ◽  
1994 ◽  
Vol 76 (6) ◽  
pp. 515-523 ◽  
Author(s):  
F. Guerlesquin ◽  
A. Dolla ◽  
M. Bruschi
Keyword(s):  
Cytochrome C ◽  
Electrostatic Interactions ◽  
C Complex ◽  
Complex Formations

Evolutionary alkaline transition in human cytochrome c

2009 ◽  
Vol 41 (3) ◽  
pp. 251-257 ◽  
Author(s):  
Tianlei Ying ◽  
Fangfang Zhong ◽  
Jin Xie ◽  
Yanjiao Feng ◽  
Zhong-Hua Wang ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Alkaline Transition ◽  
Human Cytochrome ◽  
Human Cytochrome C

scholarly journals Importance of the redox state of cytochrome c during caspase activation in cytosolic extracts

1998 ◽  
Vol 329 (1) ◽  
pp. 95-99 ◽  
Author(s):  
B. Mark HAMPTON ◽  
Boris ZHIVOTOVSKY ◽  
F. G. Andrew SLATER ◽  
H. David BURGESS ◽  
Sten ORRENIUS
Keyword(s):  
Cytochrome C ◽  
Electrostatic Interactions ◽  
Ionic Composition ◽  
Binding Pocket ◽  
Caspase Activation ◽  
Binding Partner ◽  
Allosteric Interactions ◽  
Transport Chain ◽  
Intracellular Signal ◽  
Chain Interaction

The export of cytochrome c from mitochondria to the cytoplasm has been detected during apoptosis. Addition of cytochrome c to cytosolic extracts can activate the caspases, suggesting that this export could be an important intracellular signal for initiating the apoptotic programme. We have investigated the mechanism of caspase activation by cytochrome c. Mitochondrial cytochrome c normally shuttles electrons between complexes III and IV of the electron transport chain. Interaction with these complexes is dependent on electrostatic interactions via a polylysine binding pocket. Cytosolic caspase activation was only observed with intact holocytochrome c, and increasing the ionic composition of the extracts prevented activation, suggesting that stringent allosteric interactions between cytochrome c and other cytoplasmic factors are necessary. Cytochrome c was fully reduced within 5 min of addition to the cytosolic extracts. Potassium ferricyanide could maintain cytochrome c in an oxidized state, but care was taken to use ferricyanide at concentrations where its polyanion effect did not cause interference. The oxidized form of cytochrome c was able to activate the caspases. We conclude that reduced cytochrome c will function in the cytoplasm; however, its reduction is not a critical step, and electron transfer from cytochrome c to its cytoplasmic-binding partner(s) is not necessary in the pathway leading to apoptosis.

Sign in / Sign up

Export Citation Format

Share Document