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Section 9: Oxidative Phosphorylation, Summaries of Biological Sciences

Explain the benefits of having the electron-transport chain located in a membrane. ✓ Described how the proton-motive force is converted into ATP.

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Section9:OxidativePhosphorylation
Chapter20:TheElectronTransportChain
Chapter21:TheProtonMotiveForce
LearningObjectives
Bytheendofthissection,youshouldbeableto:
Describethekeycomponentsoftheelectrontransportchainand
howtheyarearranged
Explainthebenefitsofhavingtheelectrontransportchainlocated
inamembrane
DescribedhowtheprotonmotiveforceisconvertedintoATP
Identifytheultimatedeterminantoftherateofcellularrespiration
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Section

^9 :^ Oxidative

Phosphorylation

-^ Chapter

20:^ The

Electron

‐Transport

Chain

-^ Chapter

21:^ The

Proton

‐Motive

Force

Learning

Objectives

By^ the

end^ of

this^ section,

you^ should

be^ able

to:

^ Describe

the^ key

components

of^ the

electron

transport

chain

and

how^ they

are^ arranged

^ Explain

the^ benefits

of^ having

the^ electron

‐transport

chain

located

in^ a^ membrane  Described

how^ the

proton

‐motive

force^

is^ converted

into^ ATP

^ Identify

the^ ultimate

determinant

of^ the

rate^ of

cellular

respiration

Lecture:

‐^09

‐^2016

CHAPTER

The^

Electron

‐Transport

Chain

Chapter

Outline

-^ Oxidative

phosphorylation

captures

the^ energy

of^ high

‐energy

electrons

to^ synthesize

ATP.

-^ The flow^ of

electrons

from^ NADH

and^ FADH

to^ O 2 2 occurs

in^ the

electron

‐transport

chain^

or^ respiratory

chain.

-^ This

exergonic

set^ of^

oxidation

‐reduction

reactions

generates

a^ proton

gradient. • The^ proton

gradient

is^ used

to^ power

the^ synthesis

of^ ATP.

-^ Collectively,

the^ citric

acid^ cycle

and^ oxidative

phosphorylation

are

called^

cellular

respiration

or^ simply

respiration

cellular

respiration

Electron micrograph (A)and diagram (B) of a mitochondrion

-^ The

outer^

mitochondrial

membrane

is^ permeable

to^ most

small^ ions

and

molecules

because

of^ the

channel

protein

mitochondrial

porin.

-^ The

inner^ membrane,

which

is

folded^

into^ ridges

called cristae,

is

impermeable

to^ most

molecules.

-^ The

inner^ membrane

is^ the^

site^ of

electron

transport

and^ ATP synthesis. • The^ citric

acid^ cycle

and^ fatty

acid

oxidation

occur^

in^ the^ matrix.

Biological

Insight:

Sequence

data^ suggest

that

all^ mitochondria

are^ descendants

of^ an

ancestor

of^ Rickettsia

prowazekii

,^ which^ was

engulfed

by^ another

cell.^

The^ reduction

potential

E ′,^ or^0 redox^

potential,

is^ a^ measure

of^ a^ molecule’s

tendency

to^ donate

or^ accept

electrons.

A^ strong

reducing

agent^

readily

donates

electrons

and^ has

a^ negative

E ′.^0

A^ strong

oxidizing

agent^

readily

accepts

electrons

and^ has

a^ positive

E ′.^0

The^ standard

free‐energy

change

is^ related

to^ the

change

in^ reduction

potential. where^

n^ is^ the

number

of^ electrons

transferred

and^ F^

is^ the^ Faraday

constant.

Energy

is^ released

when^

high‐energy

electrons

are^ transferred

to^ oxygen.

The^ energy

is^ used

to^ establish

a^ proton

gradient.

-^ The

electron

‐transport

chain^

is^ composed

of^ four

large^ protein

complexes. • The^ electrons

donated

by^ NADH

and^ FADH

are^ passed 2

to^ electron

carriers

in^ the protein

complexes.

-^ The

carriers

include

flavin mononucleotide

(FMN),

iron^ associated

with

sulfur^ in

proteins

(iron‐sulfur

proteins),

iron^ incorporated

into^ hemes that

are^ embedded

in^ proteins

called cytochromes,

and^ a^

mobile

electron

carrier

called

coenzyme

Q^ (Q).

-^ Electron

flow^ within

the^ complexes

in^ the^

inner‐mitochondrial

membrane

generate

a^ proton

gradient.

-^ These

complexes

appear

to^ be^ associated

with^ one

another

in^ what

is

called^ the^ respirasome.

Iron–sulfur clusters

(A)^ A single iron ion bound by four cysteine residues.

(B)^ 2Fe-2S cluster with iron ions bridged

by sulfide ions.

(C)^ 4Fe-4S cluster. Each of these clusters can undergo oxidation–reduction reactions. •^ Frataxin

is^ a^ mitochondrial

protein

required

for^ the

synthesis

of^ iron

‐sulfur

clusters. • Loss^ of

frataxin

results

in^ Friedreich’s

ataxia,

a^ disease

that^ affects

the^ nervous

system

as^ well

as^ the

heart^

and^ skeletal

system.

-^ Coenzyme

Q^ is^ derived

from^ isoprene.

-^ Coenzyme

Q^ binds

protons

(QH)^2

as^ well

as

electrons,

and^ can

exist^ in

several

oxidation

states. • Oxidized

and^ reduced

Q^ are^

present

in^ the

inner^ mitochondrial

membrane

in^ what

is

called^

the^ Q^ pool.

-^ The

electrons

from^ NADH

are^ passed

along^

to^ Q^ to

form^ QH

by^ Complex 2

I.^ QH^2

leaves^

the^ enzyme

for^ the

Q^ pool

in^ the^

hydrophobic

interior

of^ the

inner‐

mitochondrial

membrane.

-^ Four

protons

are^ simultaneously

pumped

out^ of

the^ mitochondria

by^ Complex

I. 17

Electrons

from^ QH

are^ used 2

to^ reduce

two^ molecules

of^ cytochrome

c^ in

a^ reaction

catalyzed

by^ the

Q‐cytochrome

c^ oxidoreductase or

Complex

III.^ Complex

III^ is^ also

a^ proton

pump.

•^ QH

carries 2

two^ electrons

while^

cytochrome

c^ carries

only^ one

electron.

-^ The

mechanism

for^ coupling

electron

transfer

from^ QH

to^ cytochrome 2

c^ is

called^ the^ Q^ cycle.

-^ In^ one

cycle,^

four^ protons

are^ pumped

out^ of

the^ mitochondria

and^ two

more

are^ removed

from^ the

matrix.

•^ QH

carries 2

two^ electrons

while^

cytochrome

c^ carries

only^ one

electron.

-^ The

mechanism

for^ coupling

electron

transfer

from^ QH

to^ cytochrome 2

c^ is

called^ the^ Q^ cycle

Definition: •^ The

Q^ cycle

is^ a set

of^ reactions

in^ which

coenzyme

Q^ cycles

between

the

fully^ reduced

state^ and

the^ fully

oxidized

state^ through

one‐electron

transfer

reactions

in^ which

one^ of

the^ electrons

is^ temporarily

stored

in;

provides

a^ means

of^ passing

the^ two

electrons

of^ coenzyme

Q^ to^ the

single‐

electron

carrier

cytochrome

c ,^ one

electron

at^ a^ time.

-^ In^ one

cycle,^

four^ protons

are^ pumped

out^ of

the^ mitochondria

and^ two

more^ are

removed

from^ the

matrix.