Bio 107 topic 4 Flashcards

1
Q

What type of energy do organisms absorb?

A

light or chemical

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What type of energy do organisms release?

A

thermal and metabolic wastes

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Laws of thermodynamics in terms of organisms transformation of energy

A
  • energy is neither created nor destroyed, only transferred and transformed
  • every energy transfer or transformation increases the entropy of the surroundings
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Entropy

A

randomness/disorder
- inversely related to free energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is the most disorganized form of energy?

A

heat
release of heat=increase entropy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What happens to a chemical reaction if they result in an increase in entropy?

A

the reaction will proceed spontaneously-not necessarily fast

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

The 2nd law of thermodynamics states that energy transformations increase entropy, but living things are very ordered and non-random. Explain how living things can exist without violating the second law of thermodynamics.

A

­- Cells are open systems
­- Take in energy and matter in low entropy forms → used to create localized order in the cell
­- Energy and matter are returned to surroundings in a less ordered form →Organisms decrease order of their surroundings

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What has to happen in order for a non spontaneous reaction to occur in the cell?

A

energy has to be added

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Exergonic reaction

A
  • releases free energy
  • (ΔG <0)
  • occurs spontaneously
    ex. breaking polymers into monomers
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Endergonic reaction

A
  • absorbs free energy from the surrounds to power the reaction
  • (ΔG>0)
  • non spontaneous
    ex. making a polymer from monomers
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Metabolism

A

all of an organism’s chemical reactions organized into pathways

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Metabolic pathway

A

the chemical reactions from a starting material to an ending material
- each step catalyzed by a different enzyme

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Catabolic pathway

A

type of metabolic pathway that break down complex molecules into simpler molecules
- releases energy (exergonic)
- requires enzymes
ex. breakdown of starch to glucose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Anabolic pathway

A

type of metabolic pathway that build complex molecules from simpler molecules
- requires energy (endergonic)
- requires enzymes
ex. photosynthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Energy coupling

A

energy released from one set of reactions is used to power another set of reactions that require energy
- energy release from catabolic used to power anabolic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Cellular work that relies on ATP

A
  1. Movement
    - transport vesicles around cell
    - flagella and cilia
  2. Transport
    - moves substances across membrane against concentration gradient
  3. Chemical
    - driving endergonic chemical reactions
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

ATP

A

adenosine triphosphate
- three phosphate groups
- ribose sugar
-adenine nitrogenous base
-nucleotide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Why is ATP hydrolysis exergonic?

A

repulsive forces between negatively charged phosphate groups make ATP less stable than ADP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Phosphorylation

A

phosphate from ATP hydrolysis is added to another molecule
- makes molecules more reactive causing endergonic reactions to occur

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

What can cause a protein to change shape?

A

-phosphorylation
- binding and hydrolyzing ATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

ATP cycle

A

cell constantly makes ATP by re-phosphorylation

22
Q

Electrons going from a less electronegative atom to a more electronegative atom release or absorb energy?

A

release. Sometimes it is not all used so it is stored in electron shuttle molecules

23
Q

Which type of covalent bonds have a high and low potential energy of electrons?

A

C-H: high
C-C: high
O-O: Very high
C-O: low
O-H: low

Non polar=high
Polar=low

24
Q

Redox reaction

A

reaction where there is a transfer of electrons from one reactant to another

25
Oxidation
loss of electrons
26
Reduction
gains electrons
27
Electron shuttle molecules
temporary storage site for high energy elections. Uses dehydrogenase ex. NAD+
28
Dehydrogenase
enzyme that removes 2 hydrogen atoms from high energy substrates and transfers them into shuttle molecules
29
Oxidized form NAD+
-low energy - can accept electrons
30
Reduced form (NADH)
- high energy - stores electrons
31
Electron transport chains
a series of electron-carrying membrane proteins that transfer electrons and release energy - receive high energy electrons (from electron shuttles) - release energy in small steps by redox reactions
32
Enzyme
catalytic protein that speeds up a reaction without being consumed itself
33
Enzyme properties
- increases reaction rate - does not change the reaction - does not provide energy to the reaction - used in both exergonic and endergonic reactions - activity can be regulated - lowers Ea needed for a reaction to occur without changing G
34
Substrate
reactant that an enzyme acts upon
35
Product
molecules produced at the end of the reaction
36
Active site
Pocket on the surface of the enzyme where the substrate binds and where the reaction happens - enzyme specific to its substrate due to shape of active site which is caused by amino acid sequence
37
How does an enzyme work?
1. Substrate enters the active site and enzymes change shape to interact with the substrate 2. Substrate is held in place in the active site of the enzyme -H-bonds, hydrophobic interactions, charge interactions form between active site amino acids and substrate 3. Activation energy is lowered by the active site (3 ways this can be done) a) Enzyme lines up the substrates correctly for new bonds to form b) Bonds in the substrate are stressed making them easier to break c) Creates a charge environment that favours the reaction 4. Substrate is converted into products that are released from active site o Products have a different shape than substrates, and don’t fit in active site 5. Cycle repeats
38
Induced fit
enzyme changes shape to interact with substrate
39
What factors affect enzyme activity ?
- concentration of substrate - concentration of enzyme - temperature - pH - cofactors and coenzymes - enzyme inhibitors
40
Concentration of substrate (enzyme activity)
- more substrate=faster reaction rate - rate increases until all active sits in all enzymes are full (maximum)
41
Concentration of enzyme (enzyme activity)
- more enzyme= faster reaction rate as long as there is substrate for all enzymes at max
42
Temperature (enzyme activity)
- ↑ temperature = ↑ enzyme/substrate interactions = increases reaction rate - Too much heat = enzymes denature = lower reaction rate - Optimal temperature produces fastest rate:
43
pH (enzyme activity)
- affects charges on amino acid side chains - changes in pH = changes protein shape and ability of substrate to bind in active site= decreased reaction rate - optimal pH produces
44
Cofactors
metal ions or inorganic minerals
45
Coenzymes
organic molecules (vitamins)
46
Cofactors and Coenzymes
non protein helpers that are required for catalytic activity of enzymes
47
Enzyme inhibitors
chemicals that selectively decrease activity of an enzyme ex. chemicals, drugs, poisons, normal molecules in the cell
48
Irreversible inhibitors
Type of enzyme inhibitor - bind to enzyme using covalent bonds - permanent inactivation
49
Reversible inhibitors
Type of inhibitory enzyme - bind to enzyme using hydrogen bonds - temporary inactivation (enzyme will return to normal when inhibitor removed
50
Competitive inhibitor
Type of reversible inhibitor - mimics the normal enzyme substrate - competes with substrate for binding to active site - blocks the active site and prevents formation of enzyme-substrate complex=decreased reaction rate - can be overcome by increasing substrate concentration
51
Non-competitive inhibitor
Type of reversible inhibitor - bind to region of enzyme other than the active site - changes the shape of the enzyme to make it less able to bind substrate - does not compete with substrate for active site - cannot be overcome by adding more substrate