New answers tagged enzymes
Interesting question and actually I haven't found a real answer here yet. The phages seem to bind rather hard, since the need to be blended (subjected to relatively high forces) to shear off. This was used in the Hershey-Chase-Experiment to find out what the genetic material of the cell is. It doesn't matter though, since most of the cells which are infected ...
Succinate dehydrogenase is also known as Complex II in the electron transport chain. Although textbooks often show Complex II as taking FADH2 as a substrate, this is a little bit misleading. Succinate is the substrate, the oxidation of which facilitates the reduction of an FAD cofactor, which is already bound to Complex II. The resulting FADH2 is then ...
The reason behind this lies in the properties of FAD+. Unlike NAD+, FAD+ is not free to diffuse within the mitochondrion, it is an integral part of the inner mitochondrial membrane. Its reduced form FADH2 contributes electrons directly to ETC.
Ki is the equilibration dissociation constant. The smaller this constant is, the stronger (more specific) is the binding between the inhibitor and the enzyme. If the residual concentration is now higher than the Ki, for each molecule from the inhibitor which dissociates from the enzyme a new will bind (simply because of the concentration). If the ...
Top 50 recent answers are included