You can use the equation ΔS(surr)=q(surr)/T or ΔS(surr)=-q(rxn)/T.
the two equations are equal since we know that the energy the system (reactoin) puts out just goes into the surroundings.
(In other words q(surr)=-q(rxn))
Using the equation, <span>ΔS(surr)=-(-283kJ/298K)=0.9497kJ/K or 949.7J/K
This answer makes sense since the reaction is exothermic which means it released energy into the system which usually causes the entropy to increase.
I hope that helps.</span>
Chemical equilibrium is reach when the concentrations of the product and reactants will no longer change with time. this does not mean that there is no change in concentration, only the net change is zero. the forward rate of reaction is now equal to backward rate of reaction.
Answer:
1 : 2 ratio
Explanation:
Chlorine has a coefficient of 1, and sodium chloride has a coefficient of 2.
Answer:
The lock-and-key model:
c. Enzyme active site has a rigid structure complementary
The induced-fit model:
a. Enzyme conformation changes when it binds the substrate so the active site fits the substrate.
Common to both The lock-and-key model and The induced-fit model:
b. Substrate binds to the enzyme at the active site, forming an enzyme-substrate complex.
d. Substrate binds to the enzyme through non-covalent interactions
Explanation:
Generally, the catalytic power of enzymes are due to transient covalent bonds formed between an enzyme's catalytic functional group and a substrate as well as non-covalent interactions between substrate and enzyme which lowers the activation energy of the reaction. This applies to both the lock-and-key model as well as induced-fit mode of enzyme catalysis.
The lock and key model of enzyme catalysis and specificity proposes that enzymes are structurally complementary to their substrates such that they fit like a lock and key. This complementary nature of the enzyme and its substrates ensures that only a substrate that is complementary to the enzyme's active site can bind to it for catalysis to proceed. this is known as the specificity of an enzyme to a particular substrate.
The induced-fit mode proposes that binding of substrate to the active site of an enzyme induces conformational changes in the enzyme which better positions various functional groups on the enzyme into the proper position to catalyse the reaction.
Helium is the least reactive because it has the least protons
