What is unique about cytochrome c?
Cytochrome c is highly water-soluble, unlike other cytochromes, and is an essential component of the electron transport chain, where it carries one electron. It is capable of undergoing oxidation and reduction as its iron atom converts between the ferrous and ferric forms, but does not bind oxygen.
What is the biological significance of cytochrome?
Cytochromes are proteins that contain heme as their prosthetic group and whose principal biological function, in the cells of animals, plants, and microorganisms, is electron transport.
What is the main function of cytochrome?
Cytochrome c is primarily known for its function in the mitochondria as a key participant in the life-supporting function of ATP synthesis. However, when a cell receives an apoptotic stimulus, cytochrome c is released into the cytosol and triggers programmed cell death through apoptosis.
Where is cytochrome a found?
mitochondria
Introduction. Cytochromes are a class of heme-containing proteins found in bacteria and the mitochondria of eukaryotes. These proteins are generally membrane-bound and are known as respiratory pigments because they are involved in various electron transport systems in oxidative phosphorylation.
What happens when cytochrome P450 is inhibited?
Cytochrome P450 enzymes are essential for the metabolism of many medications. Cytochrome P450 enzymes can be inhibited or induced by drugs, resulting in clinically significant drug-drug interactions that can cause unanticipated adverse reactions or therapeutic failures.
Where are cytochromes found?
mitochondrial
In healthy cells, cytochrome c (Cyt c) is located in the mitochondrial intermembrane/intercristae spaces, where it functions as an electron shuttle in the respiratory chain and interacts with cardiolipin (CL).
Do cytochromes contain iron?
The iron in cytochromes usually exists in a ferrous (Fe2+) and a ferric (Fe3+) state with a ferroxo (Fe4+) state found in catalytic intermediates. Cytochromes are, thus, capable of performing electron transfer reactions and catalysis by reduction or oxidation of their heme iron.
What can trigger cytochrome release from mitochondria?
In the first case, mitochondrial Ca2+ overload promotes the opening of the permeability transition pore. In particular, the oligomeric form of the pro-apoptotic protein Bax stimulates cytochrome c release, although the precise way in which this protein permeabilizes the outer mitochondrial membrane remains unclear.
Why are there so many unexplained mysteries in the world?
Unexplained Mysteries. The universe is full of unexplained mysteries, and in the words of Aristotle, “The more you know, the more you know you don’t know.” Mysteries drive us to explore, to search, to think and experiment.
Who was the first person to describe cytochromes?
Cytochromes were initially described in 1884 by MacMunn as respiratory pigments (myohematin or histohematin). In the 1920s, Keilin rediscovered these respiratory pigments and named them the cytochromes, or “cellular pigments”.
How are the different types of cytochromes distinguished?
Several kinds of cytochrome exist and can be distinguished by spectroscopy, exact structure of the heme group, inhibitor sensitivity, and reduction potential. Four types of cytochromes are distinguished by their prosthetic groups:
How did the cytochrome P450 family get its name?
A distinct family of cytochromes is the cytochrome P450 family, so named for the characteristic Soret peak formed by absorbance of light at wavelengths near 450 nm when the heme iron is reduced (with sodium dithionite) and complexed to carbon monoxide.