Cytochrome c, somatic | ||
 | ||
| Cytochrome c with heme | ||
| Available structures: 1j3s, 2b4z | ||
| Identifiers | ||
| Symbol(s) | CYCS; HCS; CYC | |
| External IDs | OMIM: 123970 MGI: 88578 HomoloGene: 68675 | |
| RNA expression pattern | ||
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| Orthologs | ||
| Human | Mouse | |
| Entrez | 54205 | 13063 |
| Ensembl | ENSG00000172115 | n/a |
| Uniprot | P99999 | n/a |
| Refseq | NM_018947 (mRNA) NP_061820 (protein) | XM_975140 (mRNA) XP_980234 (protein) |
| Location | Chr 7: 25.12 - 25.13 Mb | n/a |
| Pubmed search | [1] | [2] |
|
Cytochrome c, or cyt c (horse heart: PDB 1HRC) is a small heme protein found loosely associated with the inner membrane of the mitochondrion. The Human Genome Organisation (HUGO is an organization involved in the Human Genome Project, a project about mapping the human genome The Mouse Genome Informatics (MGI website is run by The Jackson Laboratory. HomoloGene, a tool of the National Center for Biotechnology Information (NCBI is a system for automated detection of homologs (similarity attributable to descent The Entrez Global Query Cross-Database Search System is a powerful Federated search engine or Web portal that allows users to search many discrete Health sciences Ensembl is a joint scientific project between the European Bioinformatics Institute and the Wellcome Trust Sanger Institute, which was launched in 1999 in response to the imminent UniProt is the uni versal prot ein resource a central repository of Protein data created by combining Swiss-Prot, TrEMBL PubMed is a free search engine for accessing the MEDLINE database of citations and abstracts of biomedical research articles The Protein Data Bank ( PDB) is a repository for 3-D structural data of Proteins and Nucleic acids These data typically obtained by X-ray crystallography A heme ( American English) or haem ( British English) is a Prosthetic group that consists of an Iron atom contained in the center of Proteins are large Organic compounds made of Amino acids arranged in a linear chain and joined together by Peptide bonds between the Carboxyl In Cell biology, a mitochondrion (plural mitochondria) is a membrane-enclosed Organelle found in most eukaryotic cells. It is a soluble protein, unlike other cytochromes, and is an essential component of the electron transfer chain, where it carries one electron. Cytochromes are in general membrane-bound Hemoproteins that contain Heme groups and carry out Electron transport. An electron transport chain couples a chemical reaction between an electron donor (such as NADH) and an electron acceptor (such as O2) to the transfer It is capable of undergoing oxidation and reduction, but does not bind oxygen. Redox (shorthand for reduction-oxidation reaction describes all Chemical reactions in which atoms have their Oxidation number ( Oxidation state Redox (shorthand for reduction-oxidation reaction describes all Chemical reactions in which atoms have their Oxidation number ( Oxidation state Oxygen (from the Greek roots ὀξύς (oxys (acid literally "sharp" from the taste of acids and -γενής (-genēs (producer literally begetteris the It transfers electrons between Complexes III and IV. The coenzyme Q: cytochrome c — oxidoreductase, sometimes called the cytochrome bc 1 complex, and at other times complex III The Enzyme cytochrome c oxidase or Complex IV () is a large Transmembrane protein complex found in Bacteria and the Mitochondrion It belongs to cytochrome c family of proteins. Cytochromes c (cytC are electron-transfer proteins having one or several Heme c groups bound to the protein by one or more generally two thioether bonds involving
Variation
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. The unified atomic mass unit ( u) or Dalton ( Da) or sometimes universal mass unit, is an unit of Mass used to express Cladistics is the hierarchical classification of Species based on evolutionary ancestry Its primary structure consists of a chain of 100 amino acids. In Chemistry, an amino acid is a Molecule containing both Amine and Carboxyl Functional groups In Biochemistry, this
The cytochrome c molecule has been studied for the glimpse it gives into evolutionary biology. Both chickens and turkeys have the identical molecule (amino acid for amino acid) within their mitochondria, whereas ducks possess molecules differing by one amino acid. The chicken ( Gallus gallus, sometimes G gallus domesticus) is a domesticated Fowl which is traditionally believed to have descended from Turkey (Türkiye known officially as the Republic of Turkey ( is a Eurasian Country that stretches For duck as a food see Duck (food; for other meanings see Duck (disambiguation. Similarly, both humans and chimpanzees have the identical molecule, while rhesus monkeys possess cytochromes differing by one amino acid. Human beings, humans or man (Origin 1590–1600 L homō man OL hemō the earthly one (see Humus Chimpanzee (often shortened to chimp) is the common name for the two extant Species of Apes in the Genus Pan. The Rhesus Macaque ( Macaca mulatta) often called the Rhesus Monkey, is one of the best known species of Old World monkeys Adult males measure
Functions
Cytochrome c can catalyze several reactions such as hydroxylation and aromatic oxidation, and shows peroxidase activity by oxidation of various electron donors such as 2,2-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS), 2-keto-4-thiomethyl butyric acid and 4-aminoantipyrine. Hydroxylation is any chemical process that introduces one or more hydroxyl groups (-OH into a compound (or radical thereby oxidizing it Redox (shorthand for reduction-oxidation reaction describes all Chemical reactions in which atoms have their Oxidation number ( Oxidation state Peroxidases ( EC number 1111x are a large family of Enzymes A majority of peroxidase protein sequences can be found in the PeroxiBase database In Biochemistry, 22'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid or ABTS is chemical compound used to observe the reaction kinetics of specific
Role in low level laser therapy
Cytochrome c is also suspected to be the functional complex in so called LLLT: Low-level laser therapy. In LLLT, laser light on the wavelength of 670 nanometer penetrates wounded and scarred tissue in order to increase cellular regeneration. Light of this wavelength appears capable of increasing activity of cytochrome c, thus increasing metabolic activity and freeing up more energy for the cells to repair the tissue.
Role in apoptosis
Cytochrome c is also an intermediate in apoptosis, a controlled form of cell death used to kill cells in the process of development or in response to infection or DNA damage[1] .
Cytochrome c is released by the mitochondria in response to pro-apoptotic stimuli. The sustained elevation in calcium levels precedes cyt c release from the mitochondria. Calcium (ˈkælsiəm is the Chemical element with the symbol Ca and Atomic number 20 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. Inositol triphosphate receptor ( IP3R) is a membrane Glycoprotein complex acting as Ca2+ channel activated by Inositol triphosphate The endoplasmic reticulum (Greek endo = "within" (prefix plásma = "formed entity" Latin reticulum = "little net" or ER, is an Organelle The overall increase in calcium triggers a massive release of cyt c, which then acts in the positive feedback loop to maintain ER calcium release through the IP3Rs. This explains how the ER calcium release can reach cytotoxic levels. This release in turn activates caspase 9, a cysteine protease. Caspases, or c ysteine- asp artic acid prote ases, are a family of Cysteine proteases which play essential roles in Apoptosis (programmed A protease is any Enzyme that conducts Proteolysis, that is begins protein Catabolism by Hydrolysis of the Peptide bonds that link Caspase 9 can then go on to activate caspases 3 and 7, which are responsible for destroying the cell from within.
Classes
In 1991 R. P. Ambler recognized four classes of cytochrome c:
- Class I includes the lowspin soluble cytochrome c of mitochondria and bacteria. It has the heme-attachment site towards the N terminus of histidine and the sixth ligand provided by a methionine residue towards the C terminus.
- Class II includes the highspin cytochrome c'. It has the heme-mattachment site closed to the N terminus of histidine.
- Class III comprises the low redox potential multiple heme cytochromes. The heme c groups are structurally and functionally nonequivalent and present different redox potentials in the range 0 to -400 mV.
- Class IV was originally created to hold the complex proteins that have other prosthetic groups as well as heme c.
References
- ^ Liu X, Kim C, Yang J, Jemmerson R, Wang X (1996). "Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c". Cell 86 (1): 147–57. doi:. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 8689682.
Further reading
- Skulachev VP (1998). "Cytochrome c in the apoptotic and antioxidant cascades. ". FEBS Lett. 423 (3): 275–80. PMID 9515723.
- Mannella CA (1998). "Conformational changes in the mitochondrial channel protein, VDAC, and their functional implications. ". J. Struct. Biol. 121 (2): 207–18. doi:. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 9615439.
- Ferri KF, Jacotot E, Blanco J, et al. (2001). "Mitochondrial control of cell death induced by HIV-1-encoded proteins. ". Ann. N. Y. Acad. Sci. 926: 149–64. PMID 11193032.
- Britton RS, Leicester KL, Bacon BR (2002). "Iron toxicity and chelation therapy. ". Int. J. Hematol. 76 (3): 219–28. PMID 12416732.
- Haider N, Narula N, Narula J (2003). "Apoptosis in heart failure represents programmed cell survival, not death, of cardiomyocytes and likelihood of reverse remodeling. ". J. Card. Fail. 8 (6 Suppl): S512–7. doi:. A digital object identifier ( DOI) is a permanent identifier given to an Electronic document. PMID 12555167.
- Castedo M, Perfettini JL, Andreau K, et al. (2004). "Mitochondrial apoptosis induced by the HIV-1 envelope. ". Ann. N. Y. Acad. Sci. 1010: 19–28. PMID 15033690.
- Ng S, Smith MB, Smith HT, Millett F (1977). "Effect of modification of individual cytochrome c lysines on the reaction with cytochrome b5. ". Biochemistry 16 (23): 4975–8. PMID 199233.
- Lynch SR, Sherman D, Copeland RA (1992). "Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase. ". J. Biol. Chem. 267 (1): 298–302. PMID 1309738.
- Garber EA, Margoliash E (1990). "Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition. ". Biochim. Biophys. Acta 1015 (2): 279–87. PMID 2153405.
- Bedetti CD (1985). "Immunocytochemical demonstration of cytochrome c oxidase with an immunoperoxidase method: a specific stain for mitochondria in formalin-fixed and paraffin-embedded human tissues. ". J. Histochem. Cytochem. 33 (5): 446–52. PMID 2580882.
- Tanaka Y, Ashikari T, Shibano Y, et al. (1988). "Construction of a human cytochrome c gene and its functional expression in Saccharomyces cerevisiae. ". J. Biochem. 103 (6): 954–61. PMID 2844747.
- Evans MJ, Scarpulla RC (1989). "The human somatic cytochrome c gene: two classes of processed pseudogenes demarcate a period of rapid molecular evolution. ". Proc. Natl. Acad. Sci. U. S. A. 85 (24): 9625–9. PMID 2849112.
- Passon PG, Hultquist DE (1972). "Soluble cytochrome b 5 reductase from human erythrocytes. ". Biochim. Biophys. Acta 275 (1): 62–73. PMID 4403130.
- Dowe RJ, Vitello LB, Erman JE (1984). "Sedimentation equilibrium studies on the interaction between cytochrome c and cytochrome c peroxidase. ". Arch. Biochem. Biophys. 232 (2): 566–73. PMID 6087732.
- Michel B, Bosshard HR (1984). "Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase. ". J. Biol. Chem. 259 (16): 10085–91. PMID 6088481.
- Broger C, Nałecz MJ, Azzi A (1980). "Interaction of cytochrome c with cytochrome bc1 complex of the mitochondrial respiratory chain. ". Biochim. Biophys. Acta 592 (3): 519–27. PMID 6251869.
- Smith HT, Ahmed AJ, Millett F (1981). "Electrostatic interaction of cytochrome c with cytochrome c1 and cytochrome oxidase. ". J. Biol. Chem. 256 (10): 4984–90. PMID 6262312.
- Geren LM, Millett F (1981). "Fluorescence energy transfer studies of the interaction between adrenodoxin and cytochrome c. ". J. Biol. Chem. 256 (20): 10485–9. PMID 6270113.
- Favre B, Zolnierowicz S, Turowski P, Hemmings BA (1994). "The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo. ". J. Biol. Chem. 269 (23): 16311–7. PMID 8206937.
- Gao B, Eisenberg E, Greene L (1996). "Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate. ". J. Biol. Chem. 271 (28): 16792–7. PMID 8663341.
Additional images
 ETC |  ETC |
See also
External links
- UMich Orientation of Proteins in Membranes families/superfamily-78 - Calculated orientations of cytochromes c in the lipid bilayer
- MeSH Cytochrome+c
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