Biology 1

Front 1

BIOCHEMISTRY

Back 1

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Front 2

Thermodynamics

Back 2

^(change in) G (free energy) = H (enthalpy-potential energy) - T (temp)^S (entropy)

(-)^G = spontaneous reaction: decrease ^H, increase ^S

(+) ^G = Non-spontaneous reaction

^G = 0: equilibrium

Front 3

Reaction Coordinate Graph

Back 3

Front 4

Activation Energy (Ea)

Back 4

Energy required to tech transition state (TS)

Increased Ea = Decreased rate of reaction

Front 5

Catalyst

Back 5

Increases rate of reaction

Stabilizes transition state

Front 6

Key Words

Back 6

Thermodynamics: Spontaneous, ^G, Reactants-->Products

Kinematics: Catalyst, Ea, rate

Front 7

Enzymes

Back 7

- Biological catalyst
- 3 main functions
1) increases rate of reaction
2) does not get used up
3) highly specific
- Structure: Proteins (99.8%)

Front 8

Regulations

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1) Phosphorylation
2) Proteolytic Cleavage
3) Allosteric Regulation
4) Association without polypeptides
5) Feedback Inhibition

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1) Phosphorylation

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Covalent Modification
Kinase: Takes P from ATP
Phosphorylases: Free floating Pi

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2) Proteolytic Cleavage

Back 10

Cleaves an enzyme with a protease
Zymogenens: Digestive enzymes

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3) Allosteric Regulation

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Allosteric regulator

Front 12

4) Association without polypeptides

Back 12

Cooperatively: hemoglobin

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5) Feedback Inhibition

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Front 14

Basic Kinetics

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Rate of the product forming
Reaction rate (V): rate of product per unit of time

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Enzyme Kinetics

Back 15

Enzyme concentration [E] never changes
1) [E] >> [S]
2) [E] = [S]
3) [E] << [S] - saturated: all enzyme active sites filled

Vmax = Saturation reached
Km = Vmax/2 : The affinity the substrate has for the enzyme

Front 16

Cooperativity

Back 16

Hemoglobin not an enzyme but acts like one!

1) [E] >> [S] - hard to take off
2) [E] = [S]
3) [E] << [S]

As Km increases = affinity decreases
Low affinity hard to bind

Front 17

Inhibitors

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Reduce the amount of product formed
Assume reversibility
2 Types
1) Competitive
2) Non-competitive

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1) Competitive Inhibitor

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Binds to active site
Vmax stays the same
Km will increase

Front 19

2) Non-competitive Inhibitor

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Binds to allosteric site
Vmax changes
Km stays the same

Front 20

CELLULAR RESPIRATION

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Front 21

Oxidation

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1) lose H+
2) lose e-
3) gain O2

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Reduction

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1) gain H+
2) gain e-
3) lose O2

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Glycolysis

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Location: Cytoplasm
O2 Requirement: Anaerobic
Molecules formed/used (ATP equivalents):
-2 ATP (-2 ATP)
4 ATP (4 ATP)
2 NADH (3 ATP in eukaryotes, 5 ATP in prokaryotes)

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Pyruvate Dehydroginase Complex (PDC)

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Location: Matrix of mitochondria
O2 Requirement: Aerobic (indirect)
Molecules formed/used (ATP equivalents):
2 NADH (5 ATP)

Front 25

Krebs Cycle

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Location: Matrix of mitochondria
O2 Requirement: Aerobic (indirect)
Molecules formed/used (ATP equivalents):
6 NADH (15 ATP)
2 FADH2 (3 ATP)
2 GTP (2 ATP)

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Electron Transport Chain

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Location: Inter membrane of mitochondria
O2 Requirement: Aerobic (direct)

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Oxidative Phosphorylation

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Location: Inter membrane of mitochondria
O2 Requirement: Aerobic (direct)

Front 28

# of protons = 1 ATP
???

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4 H+ = 1 ATP

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Fermentation (no oxygen)

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Front 30

Starvation

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B (beta) - Oxydation
Takes place in mitochondria
Breaks down lipids (fatty acids)
2C chains break down --> goes directly to Krebs cycle