Covalent compounds share with each other, whilst Ionic compounds take from each other.
Covalent compounds are composed of 2 or more NONMETALS.
So, it would be CO, since the rest of the compounds contain metals in them.
Answer:
∆H° = 790 kJ/mol
Explanation:
Hello,
In this case, by using the Hess law, we should handle the given reactions as shown below:
- The reaction:
2 Sr(s) + O₂ (g) → 2 SrO (s)
Should be inverted as:
2 SrO (s) → 2 Sr(s) + O₂ (g)
So the enthalpy of reaction changes to ∆H° = 1184 kJ/mol
- The reaction:
CO₂ (g) → C (s) + O₂ (g)
Should be also inverted as:
C (s) + O₂ (g) → CO₂ (g)
So the enthalpy of reaction changes to ∆H° = -394 kJ/mol
- Then, we add the modified reactions to obtain the desired reaction:
2 SrO (s) + C (s) + O₂ (g) → 2 Sr(s) + O₂ (g) CO₂ (g)
C(s) + 2 SrO(s) → CO₂ (g) + 2 Sr(s)
Therefore, the resulting enthalpy of reaction is:
∆H° = 1184 kJ/mol - 394 kJ/mol
∆H° = 790 kJ/mol
Best regards.
It’s Neon (Ne). You know because there are 10 protons and the number of protons is equal to the atomic number of an element. (Neon is #10 on the periodic table)
Answer:
A. the rate of the acylation reaction being faster than the deacylation reaction.
Explanation:
Chymotrypsin belongs to a class of enzymes known as proteases; enzymes that catalyse the cleavage of peptide bonds by hydrolysis.
The mechanism of chymotrypsin catalysis occurs in two distinct phases; (1) an acylation phase where the peptide bond is cleaved and an ester linkage is formed between the peptide carbonyl carbon and the enzyme, (2) a deacylation phase where the ester linkage is hydrolyzed and the non-avylated enzyme is regenerated.
In studies by B.S. Hartley and B.A. Kilby in 1954 of chymotrypsin hydrolysis of the ester p-nitropheylacetate, as measured by the release of nitrophenol, it was discovered that it proceeded with a burst before leveling of to a slower rate. This burst was due to a rapid acylation of all the enzyme molecules with a slow deacylation limiting the turnover of the enzyme.
Similarly, the observation of burst kinetics in rapid kinetic studies of the hydrolysis of p-nitrophenylphosphate by chymotrypsin is due to the initial phase of acylation proceeding much faster than the later phase of deacylation of the enzyme.