Plants, animals, and many unicellular organisms.
The sustained elevation in calcium levels precedes cyt c release from the mitochondria. The release of small amounts of cyt c leads to an interaction with the IP3 receptor (IP3R) on the endoplasmic reticulum (ER), causing ER calcium release. This explains how the ER calcium release can reach cytotoxic levels. This release of cytochrome c in turn activates caspase 9, a cysteine protease. Caspase 9 can then go on to activate caspase 3 and caspase 7, which are responsible for destroying the cell from within. Function [edit]. Cytochrome c is a component of the electron transport chain in mitochondria. The heme group of cytochrome c accepts electrons from the bc1 complex and transfers electrons to the complex IV. Cytochrome c is also involved in initiation of apoptosis. This explains how the ER calcium release can reach cytotoxic levels. This release of cytochrome c in turn activates caspase 9, a cysteine protease. Caspase 9 can then go on to activate caspase 3 and caspase 7, which are responsible for destroying the cell from within. Cytochrome c oxidase deficiency is caused by mutations in one of at least 14 genes. In humans, most genes are found in DNA in the cell's nucleus (nuclear DNA). However, some genes are found in DNA in specialized structures in the cell called mitochondria. This type of DNA is known as mitochondrial DNA (mtDNA). 5 The release of mitochondrial cytochrome c into the cytoplasm stimulates apoptosis and is commonly used as an indicator of the apoptotic process in the cell. 6 Serum cytochrome c levels may be an indicator of therapy-induced cell death burden 7. The transition of cytochrome c between the ferrous and ferric states within the cell, makes it an efficient biological electron-transporter and it plays a vital role in cellular oxidations in both plants and animals. Cytochrome c is a highly conserved protein across the spectrum of species, found in plants, animals, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), makes it useful in studies of cladistics. Its primary structure consists of a chain of about 100 amino acids. This explains how the ER calcium release can reach cytotoxic levels. This release of cytochrome c in turn activates caspase 9, a cysteine protease. Caspase 9 can then go on to activate caspase 3 and caspase 7, which are responsible for destroying the cell from within. Some DNA sequences code for mRNA which, in turn, codes for the amino acid sequence of proteins. Cytochrome C is a protein involved in using energy in the cell. Cytochrome C is found in most, if not all, known eukaryotes. Over time, random mutations in the DNA sequence occur. As a result, the amino acid sequence of Cytochrome C also changes. Cells without usable Cytochrome C are unlikely to survive. METHOD: A. Compare the amino acid sequence of Cytochrome C in various organisms. 1. Mark the amino acids which are different Use the example to show you how. The enzyme cytochrome c oxidase, or Complex IV (EC 1.9.3.1), is a large transmembrane protein complex found in bacteria and the mitochondrion of eukaryotes. It is the last enzyme in the respiratory electron transport chain of mitochondria or bacteria located in the mitochondrial or bacterial membrane. In mammals, eleven subunits are nuclear in origin, and three are synthesized in the mitochondria. The complex contains two hemes, a cytochrome a and cytochrome a3, and two copper centers, the Cu A and Cu B centers. In fact, the cytochrome a 3 and Cu B form a binuclear center that is the site of oxygen reduction. The initial release of cytochrome c into the cytoplasm can result in the association of cytochrome c with the inositol-3-phosphate receptor (IP3 receptor) which acts as a calcium channel on the outer membrane of the endoplasmic reticulum. The transition of cytochrome c between the ferrous and ferric states within the cell, makes it an efficient biological electron-transporter and it plays a vital role in cellular oxidations in both plants and animals. Electron Transport. Cytochrome c is primarily known as an electron-carrying mitochondrial protein. The transition of cytochrome c between the ferrous and ferric states within the cell, makes it an efficient biological electron-transporter and it plays a vital role in cellular oxidations in both plants and animals.
https://en.wikipedia.org/wiki/Cytochrome_c https://en.wikipedia.org/wiki/Cytochrome_c http://ghr.nlm.nih.gov/condition/cytochrome-c-oxidase-deficiency http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/learning-center/cytochrome-c.html https://en.wikipedia.org/wiki/Cytochrome_c http://www.indiana.edu/%7Eensiweb/cytows.r.pdf https://en.wikipedia.org/wiki/Cytochrome_c_oxidase http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/learning-center/cytochrome-c.html http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/learning-center/cytochrome-c.html
where is Cyt c found in the cell