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TTC19
Tetratricopeptide repeat domain 19, also known as TPR repeat protein 19 or Tetratricopeptide repeat protein 19, mitochondrial is a protein that in humans is encoded by the TTC19 gene. This gene encodes a protein with a tetratricopeptide repeat (TPR) domain containing several tetratricopeptide repeat, TPRs of about 34 amino acids each. These repeats are found in a variety of organisms including bacteria, fungi and plants, and are involved in a variety of functions including protein-protein interactions. This protein is embedded in the inner mitochondrial membrane and is involved in the formation of the mitochondrial respiratory chain III. It has also been suggested that this protein plays a role in cytokinesis. Mutations in this gene cause mitochondrial complex III deficiency. Alternatively spliced transcript variants have been found for this gene. Structure The ''TTC19'' gene is located on the Locus (genetics), p arm of chromosome 17 at position 12 and it spans 46,048 base pai ...
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UQCRFS1
Ubiquinol-cytochrome c reductase, Rieske iron-sulfur polypeptide 1, also known as UQCRFS1, Rieske iron-sulfur (Fe-S) protein, Cytochrome b-c1 complex subunit 5, or Complex III subunit 5 is a protein which in humans is encoded by the ''UQCRFS1'' gene. UQCRFS1 is a subunit of the respiratory chain protein Ubiquinol Cytochrome c Reductase (UQCR, Complex III or Cytochrome bc1 complex), which consists of the products of one mitochondrially encoded gene, MTCYTB (mitochondrial cytochrome b) and ten nuclear genes UQCRC1, UQCRC2, Cytochrome C1, UQCRFS1 (this protein, a type of Rieske protein), UQCRB, ("11kDa protein"), UQCRH (cyt c1 Hinge protein), UCRC ("cyt. c1 associated protein"), and ("Rieske-associated protein"). Structure ''UQCRFS1'' is located on the q arm of chromosome 19 in position 12, has 2 exons, and spans 5,969 base pairs. The ''UQCRFS1'' gene produces a 29.7 kDa protein composed of 274 amino acids. UQCRFS1 is a subunit of the respiratory chain protein Ubiquinol C ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid resid ...
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MT-CYB
Cytochrome b is a protein that in humans is encoded by the ''MT-CYB'' gene. Its gene product is a subunit of the respiratory chain protein ubiquinol–cytochrome ''c'' reductase (UQCR, complex III or cytochrome ''bc''1 complex), which consists of the products of one mitochondrially encoded gene, ''MT-CYB'' (mitochondrial cytochrome b), and ten nuclear genes—'' UQCRC1'', '' UQCRC2'', '' CYC1'', '' UQCRFS1'' ( Rieske protein), '' UQCRB'', "11kDa protein", '' UQCRH'' (cyt c1 Hinge protein), Rieske protein presequence, "cyt c1 associated protein", and Rieske-associated protein. Structure The ''MT-CYB'' gene is located on the p arm of mitochondrial DNA in position 12 and spans 1,140 base pairs. The gene produces a 42.7 kDa protein named cytochrome b composed of 380 amino acids. Cytochrome b is an integral membrane protein with hydrophobic properties. The catalytic core of the enzyme is composed of eight transmembrane helices, the iron-sulfur protein, and cytochrome c1. ...
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Cytochrome C
The cytochrome complex, or cyt ''c'', is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion. It belongs to the cytochrome c family of proteins and plays a major role in cell apoptosis. Cytochrome c is highly water-soluble, unlike other cytochromes, and is an essential component of the respiratory 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. It transfers electrons between Complexes III (Coenzyme Q – Cyt c reductase) and IV (Cyt c oxidase). In humans, cytochrome c is encoded by the ''CYCS'' gene. Species distribution Cytochrome c is a highly conserved protein across the spectrum of eukaryotic species, found in plants, animals, fungi, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), makes it useful in studies of clad ...
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Coenzyme Q
Coenzyme Q, also known as ubiquinone and marketed as CoQ10, is a coenzyme family that is ubiquitous in animals and most bacteria (hence the name ubiquinone). In humans, the most common form is coenzyme Q10 or ubiquinone-10. It is a 1,4-benzoquinone, where Q refers to the quinone chemical group and 10 refers to the number of isoprenyl chemical subunits in its tail. In natural ubiquinones, the number can be anywhere from 6 to 10. This family of fat-soluble substances, which resemble vitamins, is present in all respiring eukaryotic cells, primarily in the mitochondria. It is a component of the electron transport chain and participates in aerobic cellular respiration, which generates energy in the form of ATP. Ninety-five percent of the human body's energy is generated this way. Organs with the highest energy requirements—such as the heart, liver, and kidney—have the highest CoQ10 concentrations. There are three redox states of CoQ: fully oxidized (ubiquinone), semiquinone ...
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Catalysis
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usually gaseous or liquid) as the reactant, or heterogeneous, whose components are not in the same phase. Enzymes and other biocatalysts are often considered as a third category. Catalysis is ubiquitous in chemical industry of all kinds. Estimates are that 90% of all commercially produced chemical products involve catalysts at some st ...
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Proteins
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in ...
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Mitochondrial Genome
Mitochondrial DNA (mtDNA or mDNA) is the DNA located in mitochondria, cellular organelles within eukaryotic cells that convert chemical energy from food into a form that cells can use, such as adenosine triphosphate (ATP). Mitochondrial DNA is only a small portion of the DNA in a eukaryotic cell; most of the DNA can be found in the cell nucleus and, in plants and algae, also in plastids such as chloroplasts. Human mitochondrial DNA was the first significant part of the human genome to be sequenced. This sequencing revealed that the human mtDNA includes 16,569 base pairs and encodes 13 proteins. Since animal mtDNA evolves faster than nuclear genetic markers, it represents a mainstay of phylogenetics and evolutionary biology. It also permits an examination of the relatedness of populations, and so has become important in anthropology and biogeography. Origin Nuclear and mitochondrial DNA are thought to be of separate evolutionary origin, with the mtDNA being deri ...
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UQCRH
Cytochrome b-c1 complex subunit 6, mitochondrial is a protein that in humans is encoded by the ''UQCRH'' gene. Its gene product is a subunit of the respiratory chain protein Ubiquinol Cytochrome c Reductase (UQCR, Complex III or Cytochrome bc1 complex; E.C. 1.10.2.2), which consists of the products of one mitochondrially encoded gene, MTCYTB (mitochondrial cytochrome b) and ten nuclear genes: UQCRC1, UQCRC2, Cytochrome c1, UQCRFS1 (Rieske protein), UQCRB Ubiquinol-cytochrome c reductase binding protein, also known as UQCRB, Complex III subunit 7, QP-C, or Ubiquinol-cytochrome c reductase complex 14 kDa protein is a protein which in humans is encoded by the UQCRB gene. This gene encodes a subunit o ..., "11kDa protein", UQCRH (cyt c1 Hinge protein), Rieske Protein presequence, "cyt. c1 associated protein", and "Rieske-associated protein". References Further reading

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UQCRB
Ubiquinol-cytochrome c reductase binding protein, also known as UQCRB, Complex III subunit 7, QP-C, or Ubiquinol-cytochrome c reductase complex 14 kDa protein is a protein which in humans is encoded by the UQCRB gene. This gene encodes a subunit of the ubiquinol-cytochrome c oxidoreductase complex, which consists of one mitochondrial-encoded and 10 nuclear-encoded subunits. Mutations in this gene are associated with mitochondrial complex III deficiency. Alternatively spliced transcript variants have been found for this gene. Related pseudogenes have been identified on chromosomes 1, 5 and X. Structure ''UQCRB'' is located on the q arm of chromosome 8 in position 22.1, has 18 exons, and spans 8,958 base pairs. The ''UQCRB'' gene produces a 5.9 kDa protein composed of 161 amino acids. The gene product of UQCRB is a subunit of the respiratory chain protein Ubiquinol Cytochrome c Reductase (UQCR, Complex III or Cytochrome bc1 complex; E.C. 1.10.2.2), which consists of the pro ...
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Rieske Protein
Rieske proteins are iron–sulfur protein (ISP) components of cytochrome ''bc''1 complexes and cytochrome b6f complexes and are responsible for electron transfer in some biological systems. John S. Rieske and co-workers first discovered the protein and in 1964 isolated an acetylated form of the bovine mitochondrial protein. In 1979 Trumpower's lab isolated the "oxidation factor" from bovine mitochondria and showed it was a reconstitutively-active form of the Rieske iron-sulfur protein It is a unique Fe-2Scluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues. They have since been found in plants, animals, and bacteria with widely ranging electron reduction potentials from -150 to +400 mV. Biological function Ubiquinol-cytochrome-c reductase (also known as bc1 complex or complex III) is an enzyme complex of bacterial and mitochondrial oxidative phosphorylation systems. It catalyses the oxidation-reduction reacti ...
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Cytochrome C1
Cytochrome C1 (also known as Complex III subunit 4) is a protein encoded by the '' CYC1'' gene. Cytochrome is a heme-containing subunit of the cytochrome b-c1 complex, which accepts electrons from Rieske protein and transfers electrons to cytochrome c in the mitochondrial respiratory chain. It is formed in the cytosol and targeted to the mitochondrial intermembrane space. Cytochrome c1 belongs to the cytochrome c family of proteins. Function Cytochrome C1 plays a role in the electron transfer during oxidative phosphorylation. As an iron-sulfur protein approaches the b-c1 complex, it accepts an electron from the cytochrome b subunit, then undergoes a conformational change to attach to cytochrome c1. There, the electron carried by the iron-sulfur protein is transferred to the heme carried by cytochrome c1. This electron is then transferred to a heme carried by cytochrome c. This creates a reduced species of cytochrome c, which separates from the b-c1 complex and moves to th ...
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