Answer:
Difference in the potential energy of the reactants and products
Explanation:
The products have a lower potential energy than the reactants, and the sign of ΔH is negative. In an endothermic reaction, energy is absorbed. The products have a higher potential energy than the reactants, and the sign of ΔH is positive.
<h3>Solution-:</h3>
- option D
- maintains a constant volume.
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Answer:
Ge: [Ar] 3d10 4s2 4p2 => 6 electrons in the outer shell
Br: [Ar] 3d10 4s2 4p5 => 7 electrons in the outer shell
Kr: [Ar] 3d10 4s2 4p6 => 8 electrons in the outer shell
Explanation:
The electron affinity or propension to attract electrons is given by the electronic configuration. Remember that the most stable configuration is that were the last shell is full, i.e. it has 8 electrons.
The closer an atom is to reach the 8 electrons in the outer shell the bigger the electron affinity.
Of the three elements, Br needs only 1 electron to have 8 electrons in the outer shell, so it has the biggest electron affinity (the least negative).
Ge: needs 2 electrons to have 8 electrons in the outer shell, so it has a smaller (more negative) electron affinity than Br.
Kr, which is a noble gas, has 8 electrons and is not willing to attract more electrons at all, the it has the lowest (more negative) electron affinity of all three to the extension that really the ion is so unstable that it does not make sense to talk about a number for the electron affinity of this atom.
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Answer:
When C1 is labeled in glucose, it ends up in the methyl group of pyruvate.
Aldolase cleaves a hexose into two trioses.
[See the image attached].
Asterisk indicates the label.
When C1 is labeled in glucose, it ends up in the carboxyl group of pyruvate.
Answer:
True
Explanation:
In an uncompetitive inhibition, initially the substrate [S] binds to the active site of the enzyme [E] and forms an enzyme-substrate activated complex [ES].
The inhibitor molecule then binds to the enzyme- substrate complex [ES], resulting in the formation of [ESI] complex, thereby inhibiting the reaction.
This inhibition is called uncompetitive because the inhibitor does not compete with the substrate to bind on the active site of the enzyme.
Therefore, in an uncompetitive inhibition, the inhibitor molecule can not bind on the active site of the enzyme directly. The inhibitor can only bind to the enzyme-substrate complex formed.
