Energy and Enzyme exam 3

One characteristic of

life is

all life takes

in and uses energy

Energy

the ability to

do work/move

matter/supply heat

Potential energy

stored energy

available to do work

Kinetic energy

energy

being used to do work

potential energy

Top of hill

Kinetic energy

Coasting downhill

Non polar have higher or lower potential energy

Higher

Does polar molecule have high potential energy?

No

Chrmical bonds, chemical and electrical gradients

Potential energy

Thermal and heal, solar

Kinetic energy

law - energy cannot be

created or destroyed, can be

converted to other forms

1st law

law – all spontaneous

reactions increase entropy of

the system and/or its environment

2nd law

Study of energy tranformation

Themodynamics

true or false

Energy transformation are completely efficient

False

Describes natural phenomenon

Law

Theory

Well supported explanation of natural phenomenon

what is entropy

Disorder physical distribution and interactions of molecules

Spontaneous reactions can happen without ____ _____ of energy

Net input

Spontaneous reaction can also happen slowly, if so give me example

Diamonds to graphite

How do you know if it is sponstaneous or not

Likely spontaneous if products< potential energy than reactants (lower energy after rxn)

Products < ordered than reactants (products have increased entropy)

How happen to the difference in potentia energy?

Released often as heat

How do wwe no with more certainty whther the reaction is spontanrous?

G- gibbs free energy amount of energy in the reaction available to do work.

G= H-TdeltaS

If G is negative….

Exergonic-Reaction has energy available to do work, will be sponntaneous

Delta G is positive..

Endergonic-Energy has to be added for the reaction to happen. Wil not be spontaneous

What does each mean

T

S

H

Thermal energy, entropy, enthalpy

Enthalpy: total energy in a molecule includes potential energy and kinetic energy

How does life require macromolecules mostly produced through endergonic reactions?

Through energetic coupling between exergonic and endergonic

How does energetic coupling happen

Allowing capture of some energy from exergonic that would otherwise be released as heat.

In cells usually tranfer phosphate or electron

How does ATP store energy

Stores energy in phosphate-phosphate bonds

Phosphorylation

What does it produce

Transfering a phosphate group

It produces an activated intermediate to raise potential energy of that reactant.

Exergonic or endergonic

Exergonic

Whats redox reactions

Reduction-oxidation

Transfer of e-

Electron donor loses energy and electron recipient gains energy

Higher energy forming is Longer and waker bonds

T or F

T-Longer / weaker

To bonds to be proken and formed, it must collide.

Likelihood of collision if:

Higher temperature and more reactants required

All reaction require ____ amount of kinetic energy to _____ bonds and form a ____ state is called ____

Minimum, strain, activation energy

According to Activation energy,

Higher tempetature means_____

It is also why spontaneous reaction _____

Higher reaction rates

May not be fast

What are two hurdles for the even spontaneous reactions?

activation energy and orientation of collision

In enzyme, substrate formed? With

Glucose and ATP

activation energy needed for
the enzyme-catalyzed reaction,
• activation energy needed for
the noncatalyzed reaction,

What does each letter mean

A+B=C+D

a

Activation energy (uncatalyzed)

Energy barrier without catalyst

b

Activation energy (catalyzed)

Energy barrier with catalyst

c

Difference between a and b

Reduction in barrier due to catalyst

d

ΔG (overall free energy change)

Product energy − Reactant energy

e	Activation energy for reverse reaction

In Enzymes and activation energy, it ___ activation energy. How does it facilitates transition state?

Lowers,

shape change and

interactions between R

groups at active site and

reactants/substrates)

T or F

Many proteins need more than amino acids to function

T- ions and organic molecules often important part of enzyme active site.

Cofactors- and their example

Coenzyme-

Prosthetic groups- and their example

Cofactors are ions that reversibly interact with enzymes, minerals

Coenzymes are organic molecules that reversitbly interact

Prosthetic groups permanently attached to proteins. Many coenzyme and prosthetic groups are vitamins in your diet.

What factors that affect enzyme activity and ffunction?

Substrate concentration

Temperature

And so on( add later)

Why does the reaction rate go up with increased

temperature (at first)? Why does it start going down at

even higher temperatures?

In high temperature at first i

All active sites used means _____ at ____ substrate

Satureated, high

how does the Most enzymes have ideal temperature and p H ranges
 usually correspond well to the environment they are most
often found

natural selection.

Enzymes are highly regulated, in what way does the enzyme change shape and function? it is also calledd controlling enzyme so enzymes are not always active, so it doesn’t waste energy.

by adding phosphate groups: phosphorylation

In regulatory molecules, what are

Competitive inhibition -

Allosteric regulation -

Competitive inhibition -Inhibiting molecule may bind to
active site to block substrates

Allosteric regulation - Regulatory molecule may bind
in a different spot (not active
site) to change shape to make it active or inactive

Most enzymes don’t act alone — they work as steps in a chain of reactions, what is it called

Metabolic pathway

why does early enzyme inhibited by late(last) product in matabolic pathway? and what is it called?

It prevents the cell from overproducing molecules and saves energy and materials.
Negative feedback(feedback inhibition).

Some metabolic pathways build molecules whereas others _____

break them down.

Anabolic- build

Catabolic - break