Search results
Results from the WOW.Com Content Network
The thiourea hydrogen bonds to the nitro group and stabilizes the incoming negative charge, while the amine acts a specific base to activate the nucleophile. This is an example of bifunctional catalysis. Hydrogen-bond catalysis is a type of organocatalysis that relies on use of hydrogen bonding interactions to accelerate and control organic ...
For example, the secondary structure of the chorismate mutase of yeast is very similar to that of E. coli. Chorimate mutase in the AroQ family are more common in nature and are widely distributed among the prokaryotes. [1] For optimal function, they usually have to be accompanied by another enzyme such as prephenate dehydrogenase.
Thioureas are often found to be stronger hydrogen-bond donors (i.e., more acidic) than ureas [7] because their amino groups are more positively charged. Quantum chemical analyses revealed that this counterintuitive phenomenon, which is not explainable by the relative electronegativities of O and S, results from the effective steric size of the ...
Hydrogen bond: A hydrogen bond is a specific type of dipole-dipole interaction between a partially positive hydrogen atom and a partially negative electron donor that contain a pair of electrons such as oxygen, fluorine and nitrogen. The strength of hydrogen bond depends on the chemical nature and geometric arrangement of each group.
Researchers have since conducted increasingly detailed investigations of the triad's exact catalytic mechanism. Of particular contention in the 1990s and 2000s was whether low-barrier hydrogen bonding contributed to catalysis, [18] [19] [20] or whether ordinary hydrogen bonding is sufficient to explain the mechanism.
For example, the addition of hydrogen to ethene has a Gibbs free energy change of -101 kJ·mol −1, which is highly exothermic. [11] In the hydrogenation of vegetable oils and fatty acids, for example, the heat released, about 25 kcal per mole (105 kJ/mol), is sufficient to raise the temperature of the oil by 1.6–1.7 °C per iodine number drop.
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
A hydrogen bonds to one of the nitrogen atoms, breaking its bond with carbon, and releasing an NH 3 molecule. Simultaneously, the bond between the oxygen and the 6-coordinate nickel is broken. This leaves a carbamate ion coordinated to the 5-coordinate Ni, which is then displaced by a water molecule, regenerating the enzyme.