Answer:
Option b. Decomposition
Followed by a reduction process using charcoal
Explanation:
Lead can be obtained from lead nitrate by thermal decomposition of lead nitrate as shown below:
2Pb(NO3)2 —> 2PbO + 4NO2 + O2
The PbO obtained is reduced by charcoal(C) to obtain the metallic Pb as shown below:
2PbO + C —> Pb + CO2
Answer: The major product of the reaction between Hydrobromic Acid and 2-bromo-1-butene in the presence of ether and acid is 2,2-dibromobutane.
Explanation:
The mechanism of the reaction is supported by the Markovnikov's rule which explains that in the addition reaction of alkenes by hydrogen-halogen compounds, the incoming halogen substituent goes to the more substituted Carbon. It can also be stated that incoming hydrogen atom goes to the Carbon with more Hydrogen atoms.
The only case when the reverse of Markovnikov's rule takes place is when Hydrogen peroxide is present and the addition reagent is HBr.
This case is not like that and it simply follows the Markovnikov's rule.
I'll add an attachment of the reaction to this now.
Uranium-238 is the element that undergoes decay to yield uranium-234
Answer:
Explanation:
has a pH of 6.6, then what is the H3O+ in solution X? View Answer · What is the pOH of a solution in which (H+)
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.
