Bio315 Ch 5

Front 1

Location of "machinery" for ATP

Back 1

Cristae

Front 2

Inner and outer mitochondrial membranes enclose two spaces:

Back 2

Matrix

Intermembrane space

Front 3

Size and number of mitochondria reflects...

Back 3

Energy requirement of the cell

Front 4

Outer boundary of mitochondria

Back 4

outer mitochondrial membrane

Front 5

Glycolysis produces...

Back 5

pyruvate, NADH and 2 ATP

Front 6

Mitochondrial matrix contains...

Back 6

a circular DNA molecule, ribosomes, enzymes

Front 7

Protein content of membranes

Back 7

Outer: 50%

Inner: 75%

Front 8

large, pore-forming protein on outer membrane

Back 8

Porin

Front 9

Contained in high levels in inner membrane

Back 9

Cardiolipin

Front 10

_______&________ can be synthesized in the matrix

Back 10

RNA & proteins

Front 11

approximately ___ ATPs could be generated from a single molecule of glucose.

Back 11

36

Front 12

In the absence of O2, the pyruvate is reduced by NADH to _______

Back 12

lactate

Front 13

Tricarboxylic acid (TCA) cycle (Kreb's)

Back 13

2 carbons are oxidized into CO2, regenerating the 4-carbon oxaloacetate needed to continue the cycle

Front 14

Reduced coenzymes FADH2 and NADH are the primary products of the

Back 14

TCA cycle

Front 15

ATP formation driven by energy derived from high-energy electrons removed during substrate oxidation in pathways such as the TCA cycle, with the energy released for ATP formation by passage of electrons through the electron transport chain

Back 15

oxidative phosphorylation

Front 16

Electrons associated with either NADH or FADH2 are transferred through specific electron carriers that make up

Back 16

The electron transport chain

Front 17

Redox reactions are accompanied by a _________ in free energy

Back 17

decrease

Front 18

Transfer of electrons causes charge separation that can be measured as

Back 18

redox potential

Front 19

NADH formed during glycolysis enters the mitochondria via

Back 19

malateaspartate or glycerol phosphate shuttles

Front 20

polypeptides bound to either FAD or FMN

Back 20

Flavoproteins

Front 21

electron carrier consisting of a protein bound to a heme group - Fe or Cu metal ions

Back 21

Cytochromes

Front 22

a lipid-soluble molecule made of five-carbon isoprenoid units

Back 22

Ubiquinone

Front 23

____ Copper atoms are located within a single protein complex and alternate between Cu2+ and Cu3+

Back 23

3

Front 24

electron carrier containing Fe in association with inorganic sulfur - arranged in order of increasingly positive redox potential - sequence determined by use of inhibitors

Back 24

Iron-sulfur proteins

Front 25

(NADH dehydrogenase) catalyzes transfer of electrons from NADH to ubiquinone and transports 4 H+ per pair

Back 25

Complex I

Front 26

(succinate dehydrogenase) catalzses transfer of electrons from succinate to FAD to ubiquinone without transport of H+

Back 26

Complex II

Front 27

(cytochrome bc1) catalyzes the transfer of electrons from ubiquinone to cytochrome c and transports 4 H+ per pair

Back 27

Complex III

Front 28

(cytochrome c oxidase) catalyzes transfer of electrons to O2 and transports H+ across the inner membrane

Back 28

Complex IV

Front 29

large complex that adds four electrons to O2 to form two molecules of H2O

Back 29

Cytochrome oxidase

Front 30

Metabolic poisons CO, N3-, and CN- bind catalytic sites in complex

Back 30

IV

Front 31

Steps of oxidative phosphorylation

Back 31

1. transfer of high-energy electrons from NADH or FADH2 to electron carriers in inner membrane

2. energy release from electron transport used to pump protons from matrix to inter membrane space

Then back through ATP synthase

Front 32

concentration gradient between matrix and intermembrane space creates

Back 32

pH gradient

Front 33

energy present in both components of the gradients

Back 33

proton-motive force

Front 34

ATP synthesizing enzyme of the inner mitochondrial membrane

Back 34

ATP synthase

Front 35

Two chief components of ATP synthase

Back 35

F1 headpiece - catalytic subunit, contains 3 catalytic sites for ATP synthesis

F0 basal piece (embedded in membrane) contains a channel through which protons are conducted from the intermembrane space to the matrix - contains c-ring

Front 36

Number of c subunits in c ring

Back 36

10-14

Front 37

The binding change mechanism states:

Back 37

-movement of protons through ATP synthase alters the binding affinity of the active site

-each active site goes through distinct conformations that have different affinities for substrates and product

-there is a structural basis of catalytic site conformation

Front 38

Binding change mechanism - ___________ active sites on the catalytic subunit go through three changes;

Back 38

Beta subunit

tight, loose, or open

Front 39

Conformational change in Beta subunits is caused by

Back 39

rotation of c wheel and bound subunit

Front 40

pH open to matrix vs open to intermembrane space

Back 40

matrix: >4.25

intermembrane <4.25

Front 41

The most important factor controlling respiration rate

Back 41

ADP

Front 42

Drives transport of ADP into and ATP out of the mitochondrion

Back 42

The H+ gradient

Front 43

membrane-bound vesicles that contain oxidative enzymes

Back 43

Peroxisomes

Front 44

Peroxisomes oxidize _______________________ and synthesize _________________

Back 44

very-long-chain fatty acids

plasmalogens (phosopholipids)

Front 45

(reactive and toxic compound) is formed in peroxisomes and broken down by the enzyme catalase

Back 45

Hydrogen peroxide (H2O2)

Front 46

Mitochondrial disorders are inherited...

Back 46

maternally

Front 47

It is speculated that accumulations of mutations in mtDNA is a major cause of...

Back 47

aging

Front 48

syndrome characterized by lack of peroxisomal enzymes due to defects in translocation of proteins from the cytoplasm into the peroxisome

Back 48

Zellweger

Front 49

Caused by lack of a peroxisomal enzyme, leading to fatty acid accumulation in the brain and destruction of the myelin sheath of nerve cells

Back 49

Adrenoleukodystrophy