You have an enzymatic reaction proceeding at the optimum ph and optimum temperature. you add a competitive inhibitor to the reaction and notice that the reaction slows down.

what can you do to speed the reaction up again?

add more inhibitor to speed up the reaction.
add more substrate; it will outcompete the inhibitor and increase the reaction rate.
increase the temperature.
increase the ph.

Add more substrate.

Explanation:

First let's explain why all the other options are wrong:

A competitive inhibitor is a substance that resembles the substrate that normally reacts with the enzime, so it binds to the enzime's active sites and prevents the substrate from doing so. Adding more substrate makes it more likely than a substrate molecule binds to an enzime's active site instead of the inhibitor ("it will outcompete the inhibitor and increase the reaction rate").

the atomic number will stay the same no matter how many electrons it has, so it doesn’t decrease nor increase. it’ll only change with a different number of protons

the enthalpy of formation of water is given as -285.8kj/mol, which states that the enthalpy of formation is negative.

negative enthalpy of formation indicates that the heat is released during the reaction process. the heat is released from reaction to the surroundings the enthalpy is expressed with a negative sign with the energy given out in the reaction process.

the formation of water takes place by giving out heat which is -285.8 kj/mol.