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A protease (also called a peptidase, proteinase, or proteolytic enzyme) [1] is an enzyme that catalyzes proteolysis, breaking down proteins into smaller polypeptides or single amino acids, and spurring the formation of new protein products. [2] They do this by cleaving the peptide bonds within proteins by hydrolysis, a reaction where water ...
Photosystem II (of cyanobacteria and green plants) is composed of around 20 subunits (depending on the organism) as well as other accessory, light-harvesting proteins. Each photosystem II contains at least 99 cofactors: 35 chlorophyll a, 12 beta-carotene , two pheophytin , two plastoquinone , two heme , one bicarbonate, 20 lipids, the Mn
The antenna complex contains hundreds of chlorophyll molecules which funnel the excitation energy to the center of the photosystem. At the reaction center, the energy will be trapped and transferred to produce a high energy molecule. [2] The main function of PSII is to efficiently split water into oxygen molecules and protons.
The oxidation of water is catalyzed in photosystem II by a redox-active structure that contains four manganese ions and a calcium ion; this oxygen-evolving complex binds two water molecules and contains the four oxidizing equivalents that are used to drive the water-oxidizing reaction (Kok's S-state diagrams).
Manganese also forms strong bonds with oxygen-containing molecules such as water. The process of oxidizing two molecules of water to form an oxygen molecule requires four electrons. The water molecules that are oxidized in the manganese center are the source of the electrons that reduce the two molecules of Q to QH 2. To date, this water ...
The antenna complex is composed of molecules of chlorophyll and carotenoids mounted on two proteins. [11] These pigment molecules transmit the resonance energy from photons when they become photoexcited. Antenna molecules can absorb all wavelengths of light within the visible spectrum. [12]
A further subclass of catalytic triad variants are pseudoenzymes, which have triad mutations that make them catalytically inactive, but able to function as binding or structural proteins. [ 71 ] [ 72 ] For example, the heparin -binding protein Azurocidin is a member of the PA clan, but with a glycine in place of the nucleophile and a serine in ...
Different proteins are degraded at different rates. Abnormal proteins are quickly degraded, whereas the rate of degradation of normal proteins may vary widely depending on their functions. Enzymes at important metabolic control points may be degraded much faster than those enzymes whose activity is largely constant under all physiological ...