Search results
Results From The WOW.Com Content Network
The other hydrogen bonding network includes residues Lys120 and Asp260, as well as an ordered water molecule (with a B-factor of 16.4 Å2), which hydrogen bonds to Gly149 and Asn151 (not shown). In these two electrostatic networks, only the ε-NH 3 + group of Lys204 is the nearest to the C2 atom of DHAP (3.4 Å). [1]
After each step, Q (in the upper part of the figure) leaves the enzyme. Q-cytochrome c oxidoreductase is also known as cytochrome c reductase , cytochrome bc 1 complex , or simply complex III . [ 35 ] [ 36 ] In mammals, this enzyme is a dimer , with each subunit complex containing 11 protein subunits, an [2Fe-2S] iron–sulfur cluster and three ...
The three species all have concentrations equal to 1 / K D at pH = pK 1, for which [Cr] = 4 / K D . [3] The three lines on this diagram meet at that point. Green line Chromate and hydrogen chromate have equal concentrations. Setting [CrO 2− 4] equal to [HCrO − 4] in eq. 1, [H +] = 1 / K 1 , or pH = log K 1. This ...
The NADPH in turn maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage from compounds like hydrogen peroxide. [1] Of greater quantitative importance is the production of NADPH for tissues involved in biosynthesis of fatty acids or isoprenoids , such as the liver, mammary glands ...
The HCO 3 − and H + are ideal for buffering pH in the blood and tissues because the pKa is close to the physiological pH = 7.2 – 7.6. Since HCO 3 − and H + are regulated in the kidneys and plasma carbon dioxide is regulated in the lungs, both actions in the kidneys and lungs are important to maintain the stability of blood pH.
It contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7, [8] and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5. [9] The pH optimum for other catalases varies between 4 and 11 depending on the ...
This enzyme has been studied primarily in plants, but it has been studied in some bacteria as well. [1] It is a key enzyme in gluconeogenesis and photosynthesis that is responsible for reversing the reaction performed by pyruvate kinase in Embden-Meyerhof-Parnas glycolysis. It should not be confused with pyruvate, water dikinase.
3 dihydroorotase [2] dihydroorotate: Ring formation and Dehydration. 4 dihydroorotate dehydrogenase [3] (the only mitochondrial enzyme) orotate: Dihydroorotate then enters the mitochondria where it is oxidized through removal of hydrogens. This is the only mitochondrial step in nucleotide rings biosynthesis. 5 orotate phosphoribosyltransferase ...