Bio Mid Term 2

Front 1

Metabolism

Back 1

Sum of ALL chemical reactions that happen in a cell/living organism

Used to build or break down chemicals

Used to liberate stored energy

Front 2

Metabolical pathways

Back 2

Steps in which metabolism happens

(Each enzyme catalyzes one step)

Front 3

Metabolite

Back 3

Different molecules in a pathway

Front 4

Advantages to multi step pathways

Back 4

Changes metabolism through evolution

Ability to divert "pathway intermediates" to other pathways

Multi points allows for speed control

Front 5

1 law of thermodynamics

Back 5

Energy cna not be created or destroyed

Front 6

2nd law of thermodynamics

Back 6

Entroy increase in isolated system

every energy transfer increases the entroy in the universe.

(Energy transfer is never 100% efficient, some lost as heat)

Front 7

Entroy

Back 7

Disorder

Front 8

Free energy

Back 8

Amount of energy in "the system"

Front 9

Exergonic reaction

Back 9

Energy releasing

Happens spontaneously (but not instantaneously)

Front 10

Endergonic reactions

Back 10

Energy consuming

will NOT happen spontaneously

Energy must be put into system for it to go forward

Front 11

Example of a stable type of bond

Back 11

Covalent

Front 12

Why ATP?

Back 12

The close negative charges on the phosphate destabilizes the P-O bonds

Phosphate has negative O that dont want to be close together (put stress on bonds & makes them easier to break)

Adding H/OH makes simple new bonds

Front 13

Spontaneous reactions

Back 13

Not instantaneous dust ti energy barriers in reactions (EA)

Front 14

Activation energy (EA)

Back 14

Energy needed in order for a reaction to happen. (The top of the "hill")

Typically reached by adding heat

Front 15

How do Enzymes speed up reactions?

Back 15

By lowering EA

Add stress to specific bonds

They do NOT change ◇G (delta G)

Front 16

Active site

Back 16

Spot were enzymes bind to (lock and key, sorta)

Front 17

Induced fit model

Back 17

Is the theory maintains that the active site and the substrate are, initially, not perfect for each other.

Front 18

Substrate

Back 18

Reactant molecule

Front 19

Way for catalysis to speed up

Back 19

Hold 2 substances close together

Add stress to specific bonds

Microenvironment of active site

Facilitating H transfer

Directly participate in a reaction

Front 20

Competitive inhibition

Back 20

Other molecules blocks activation sites by bonding to it.

E.g. substrate inhibition

Front 21

Non competitive binding

Back 21

Inhibitor molecules bind elsewhere on enzyme and changes enzymes shape.

E.g. feedback inhibition

Front 22

Allosteric regulation

Back 22

For when enzymes work in complex (2+ enzymes)

Can rotate to make site unopened or open

Front 23

Allosteri Activator

Back 23

A regulatory molecule that binds to a regulatory site which stabilizes the active form

Front 24

Allosteric inhibitor

Back 24

A regulatory molecule binds to a regulatory site which stabilizes inactive form

Front 25

Cooperativty

Back 25

Substrate binds to one unit/enzyme which stabilizes the activation sit on all other units.

Front 26

Feedback inhibitor

Back 26

When you have so much of a substance the substance binds to enzyme and prevents you from making any more

Front 27

Catabolism

Back 27

Breaking something down into smaller molecules to realise energy

Front 28

Aerobic respiration

Back 28

The electrons stored in fuel molecule bonds are ultimately transferred to oxygen

Front 29

Redox reaction

Back 29

Transfer elections from one molecule to another (LEO goes GER)

Reducing agent loses election (and becomes oxidated)

Oxidizing agent receives elections (and become reduced)

Front 30

Equal vrs unequal sharing of elections

Back 30

Equal - easier to break

Unequal- harder to break

Front 31

Denaturation

Back 31

Caused by heat (hydrogen and sulfate bonds) or pH (affects ionic bonds)

Front 32

Nicoyinamide adenine dinuceotide

Back 32

NAD

Type of shuttle (e- acceptor)

Oxidizing agent

Front 33

Dehydrogenase

Back 33

Enzymes that reduce NAD to NADH

Front 34

Substrate level phosphorylation

Back 34

Direction transfer of phosphate from a substate to ADP forming ATP

Only 10% made this way

Occurs in cytosol and mitochondria

Front 35

Oxidative phosphorylation

Back 35

H gradient used to drive ATP synthase

Mitochondria only

Front 36

Glycolysis

Back 36

Starts - 1 glucose & 2 ATP, ADP

Ends - 2 pyruvate, 2 ATP, 2 NADH, 2 H2O

Happens in cytosol

Front 37

Step 1.5 Acetyl CoA production

Back 37

Start - 2 pyruvate, 2 NAD, coenzyme A

Enter mitochondria

End - release CO2, 2 NADH, 2 Acetyl CoA

Front 38

Citric acid cycle

Back 38

Krebs cyle/ the trixarboxylic acid cycle

Start - Acetyl CoA, NAD, ADP

End (x2)

- 2 CO2,

- 3 NADH,

- ATP,

- FADH2,

- Free coenzyme A

Front 39

Electron transport chain

Back 39

Energy created pumped protons (H) out of the matrix and into the cytosol

Happens in inner membrane

Electrons are moved to O2, which later is reduced to H2O

Start- O2, ADP, NADH

End - ATP, NAD, H2O

Front 40

Number of H created per susbtance in cellular respiration

Back 40

NADH - 10

FADH2 - 6

ATP - 4

Front 41

Proton motive force

Back 41

Electrochemical gradient of protons

Stored energy

Front 42

Chemiosmosis

Back 42

Osmosis of H ions

Front 43

ATP synthase

Back 43

Protein channel that spins a turbine to make ATP

Front 44

Anaerobic respiration

Back 44

Ferric iron, nitrite, or sulphate instead of O

(less electronegative therefore produce less energy)

Produces 12-26 ATP instead of 32

Front 45

Fermentation pathways

Back 45

Help recycle NADH back to NAD

Front 46

Ethanol fermentation

Back 46

Start - glucose

Process

- 2 pyruvate decarboxylated into 2 acetaldehyde (use electrons from NADH)

- regenerating NAD which can now be reused to make ATP

End

- 2 ATP

- 2 NADH

- 2 pyruvate (turned into 2 acetaldehyde)

- 2 ethonol

Front 47

Lactic acid fermentation

Back 47

2 pyruvate make lactate when reduced by electrons instead of ethanol