Bio Exam 2

Front 1

1st law of thermodynamics

Back 1

Energy can not be created or destroyed but can change form.

Front 2

ACR

Back 2

Aerobic Cellular Respiration

Front 3

Steps of ACR

Back 3

#1 Glycolysis #2 Acetyl CoA formations #3 Krebs Cycle/TCA/ Citric Acid Cycle #4 Electron Transport Chain

Front 4

Macromolecules conversion to energy

Back 4

1 Glucose- 36 ATP 1Triglyceride- 129 ATP 1 amino acid- minimal ATP's

Front 5

Anabolic RXN require?

Back 5

ATP

Front 6

Catabolic RXN?

Back 6

Produce ATP

Front 7

Key players in ACR

Back 7

Oxygen, Carbon Dioxide, Water, Electrons, Hyrdrogen

Front 8

FAD comes from

Back 8

B vitamins; Riboflavin

Front 9

FAD+2e-+2H+=

Back 9

FADH2-Full

Front 10

ATP

Back 10

Adenosine Triphosphate

Front 11

PO4

Back 11

(Pi) PO4

Front 12

ATP= ADP+?=?

Back 12

ATP=ADP+Pi = dephosphorylation

Front 13

ADP+ Pi Through ACR = ATP

Back 13

Phosphorylation

Front 14

ATP-> ADP+Pi=

Back 14

dephosphorylation

Front 15

Light RXN-

Back 15

In thylokoid in Chloroplast

Front 16

Cyclic RXN

Back 16

Needs more ATP then NADPH to run calvin cycle

Front 17

Calvin Cycle

Back 17

B phases

Front 18

Chloroplast->

Back 18

Stroma (space)

Front 19

Phase #1

Back 19

Carbon Fixation

Front 20

Phase 2

Back 20

Reduction

Front 21

Phase 3

Back 21

Regeneration of RuBP by CO2 acceptor

Front 22

ACR happens in

Back 22

both plans and animals

Front 23

Metabolic pathways

Back 23

starts with a molecule and through different steps each molecule is catalyzed by a specific enzyme.

Front 24

Catobolic pathways

Back 24

break down complex molecules to release their energy (main pathway of ACR)

Front 25

Anabolic pathways

Back 25

consume energy to build complex molecules (Also called biosynthetic pathways)

Front 26

energy

Back 26

capacity to cause change/do work.

Front 27

Thermodynamics

Back 27

study of energy transformation that occur in a collection of matter.

Front 28

The Second law of thermodynamics

Back 28

every energy transfer or transformation increases disorder (entropy) of the universe.

Front 29

entropy

Back 29

measure of disorder and randomness.

Front 30

spontaneous

Back 30

means it can occur on its own (i.e. a piece of metal rusting).

Front 31

free energy

Back 31

portion of a systems energy that can perform work when temperature and pressure are uniform throughout system.

Front 32

equilibrium

Back 32

maximum stability

Front 33

exergonic

Back 33

"energy outward" net release of free energy.

Front 34

endergonic

Back 34

absorbs free energy

Front 35

living

Back 35

not being at equilibrium with your environment

Front 36

ATP contains?

Back 36

the sugar ribose, w/nitrogenous bases adenine, and chain of three phosphate groups Pi.

Front 37

Phosphate groups are removed by?

Back 37

Hydrolysis (water splitting)

Front 38

Phosphorylated

Back 38

term applied to recipient of phosphate group. i.e. ATP-->ADP+Pi&some other molecule.

Front 39

energy coupling

Back 39

combing exergonic processes to drive endergonic processes.

Front 40

Enzyme

Back 40

macromolecule that acts as a catalyst, speeds up a rxn but isn't consumed, lowers activation energy and basically speeds up the RXN.

Front 41

Substrate

Back 41

the molecule or molecules that an enzyme acts on

Front 42

Active site

Back 42

restricted and specific area of the enzyme that binds to the substrate.

Front 43

cofactors

Back 43

many enzymes require non protein helpers for catalytic activities. (?)

Front 44

coenzyme

Back 44

organic cofactors (?)

Front 45

competitive inhibitors

Back 45

block substrates from entering active site and reduce productivity.

Front 46

How do you get rid of competitive inhibitors?

Back 46

You can increase the concentrations of substrate so when the active sites are available substrates and not inhibitors gain entry.

Front 47

Non-competitive inhibitors

Back 47

don't bind to active site; bind to a different part of te cell which causes shape change so active site is less affective

Front 48

If an inhibitor binds to and enzyme covalently what can happen?

Back 48

It can be irreversibly.

Front 49

Allosteric regulation

Back 49

a proteins function at one site is affected by the binds of regulatory molecules to a separate site. IT either stimulates or inhibits enzyme activity.

Front 50

cooperativity

Back 50

amplifies response of enzymes to subtrates and occurs when enzymes has two or more sub units and induced fit of one affects the other subunits ability to inhibit or stimulate activity.

Front 51

feedback inhibition

Back 51

metabolic pathway(s) is/are switched off by the inhibitory binding of its end products to an enzyme that acts early in a pathway.

Front 52

fermentation?

Back 52

way of degrading sugars w/o oxygen. (not the most efficient way)

Front 53

Aerobic Cellular Respiration?

Back 53

most efficient catabolic pathway, oxygen is consumed as a reactant along with organic fuel

Front 54

Anerobic respiration

Back 54

Same as ACR without O2 getting consumed. (not as efficient at all)

Front 55

Glucose (chemical equation ?)

Back 55

C6H12O6

Front 56

Break down of one mole of glucose produces how much energy?

Back 56

-689 Kcal/mol

Front 57

redox reaction is?

Back 57

electron transfers during RXN

Front 58

Oxidation

Back 58

Loss of electron from one substance to another.

Front 59

Reduction

Back 59

addition of electron from one substance to another

Front 60

oxidizing agent

Back 60

accepts the electrons

Front 61

NAD+

Back 61

electron acceptor/ carrier

Front 62

electron transport chain occurs where

Back 62

mitochondria

Front 63

glycolysis occurs where

Back 63

occurs in the cytosol begins by breaking down glucose into two molecules of pyruvate

Front 64

citric acid cycle takes place where

Back 64

in the mitochondria matrix of eukaryotic cells or cytosol of prokaryotes. completes break down of glucose by oxidizing a derivative of pyruvate to CO2

Front 65

oxidative phosphorylation

Back 65

electron transport chain and chemiosmosis

Front 66

substrate level phosphorlyation

Back 66

direct phosphoralysation of ADP

Front 67

Enzymes to what to Hydrogen atoms

Back 67

they remove them/ from the substrate.