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Plastoquinone (PQ) is a terpenoid-quinone (meroterpenoid) molecule involved in the electron transport chain in the light-dependent reactions of photosynthesis. The most common form of plastoquinone, known as PQ-A or PQ-9, is a 2,3-dimethyl-1,4- benzoquinone molecule with a side chain of nine isoprenyl units.
Coenzyme Q 10 (CoQ 10 / ˌ k oʊ k j uː ˈ t ɛ n /), also known as ubiquinone, is a naturally occurring biochemical cofactor (coenzyme) and an antioxidant produced by the human body. [ 1 ] [ 2 ] [ 3 ] It can also be obtained from dietary sources, such as meat, fish, seed oils, vegetables, and dietary supplements .
Ubiquinol (QH 2) binds to the Q o site of complex III via hydrogen bonding to His182 of the Rieske iron-sulfur protein and Glu272 of Cytochrome b. Ubiquinone (Q), in turn, binds the Q i site of complex III. Ubiquinol is divergently oxidized (gives up one electron each) to the Rieske iron-sulfur '(FeS) protein' and to the b L heme.
The cytochrome b 6 f complex is a dimer, with each monomer composed of eight subunits. [3] These consist of four large subunits: a 32 kDa cytochrome f with a c-type cytochrome, a 25 kDa cytochrome b 6 with a low- and high-potential heme group, a 19 kDa Rieske iron-sulfur protein containing a [2Fe-2S] cluster, and a 17 kDa subunit IV; along with four small subunits (3-4 kDa): PetG, PetL, PetM ...
The electrons are then transferred through the FMN via a series of iron-sulfur (Fe-S) clusters, [10] and finally to coenzyme Q10 (ubiquinone). This electron flow changes the redox state of the protein, inducing conformational changes of the protein which alters the p K values of ionizable side chain, and causes four hydrogen ions to be pumped ...
Cytochrome c 1 transfers its electron to cytochrome c (not to be confused with cytochrome c1), and the B H Heme transfers its electron to a nearby ubiquinone, resulting in the formation of a ubisemiquinone. Cytochrome c diffuses. The first ubiquinol (now oxidised to ubiquinone) is released, whilst the semiquinone remains bound. Round 2:
TCU-SMU football history. The Horned Frogs lead the all-time series between the in-state foes 53-42-7. The first-ever matchup occurred on Oct. 8, 1915, and ended in a 43-0 win for TCU in Forth ...
The iron atoms inside complex III's heme groups alternate between a reduced ferrous (+2) and oxidized ferric (+3) state as the electrons are transferred through the protein. The reaction catalyzed by complex III is the oxidation of one molecule of ubiquinol and the reduction of two molecules of cytochrome c , a heme protein loosely associated ...
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