Embed
Email

Presentation John Allen

Document Sample

Shared by: qinmei liao
Categories
Tags
Stats
views:
2
posted:
10/25/2011
language:
English
pages:
47
SBS922 Membrane Biochemistry









Mitochondria and chloroplasts





John F. Allen



School of Biological and Chemical Sciences, Queen Mary, University of

London







1

http://jfa.bio.qmul.ac.uk/lectures/

School of Biological and Chemical Sciences Seminars 2006-07

WEDNESDAYS AT 12 NOON IN LECTURE THEATRE G23,

FOGG BUILDING, SCHOOL OF BIOLOGICAL AND CHEMICAL SCIENCES









6 December 2006 PROFESSOR SO IWATA Structural studies on membrane

David Blow Chair of Biophysics proteins

and Director of Centre for

Structural Biology Division of

Molecular Biosciences, Imperial

College London, and Diamond

Light Source, Rutherford

Appleton Laboratory, Chilton







28 February 2007 Professor COLIN ROBINSON Pathways for the targeting of

Department of Biological proteins across chloroplast and

Sciences, University of Warwick, bacterial membranes

Coventry

The membrane energised state

We have seen how observed characteristics of oxidative

phosphorylation led to conclusion that there was a

membrane energised state linking electron transfer in

mitochondria to ATP synthesis and other membrane-linked

energy-dependent functions such as active transport of

solutes.

There was convincing evidence by 1960 that the transfer of energy via

this membrane energised state between the respiratory electron

transfer chain, the synthesis of ATP and the various solute transfer

systems is both efficient and fully reversible.

Membrane Energised State (cont.)

It was occurring via a common (to all these activities) and stable non-

phosphorylated energised state. This energised state was dissipated

by uncoupling agents (uncouplers), which led to a permanent increase in

the rate of electron transfer. The energised state was not dissipated by

phosphorylation inhibitors, which caused a decrease in the rate of

electron transfer which could be overcome by uncouplers.

Thus respiration will drive ATP synthesis, ATP hydrolysis will drive reversed

electron transfer, and both respiration and ATP hydrolysis will drive solute

transport. Similarly certain solute gradients of the correct magnitude and

direction will power both ATP synthesis and reversed electron transfer. It

was clear therefore that the energised state occupies a central position

in the mechanism of membrane-associated energy transduction.

This energised state was essentially linking together two

types of protein complex in coupling membranes.

a) electron transfer complexes

b) ATP synthase

Three types of coupling membranes are the IMM,

thylakoid membrane and plasma membrane of

prokaryotes, and all used same energised state.

Search for the nature of the energised state became one of

central problems in Biochemistry. Only precedent was the

phophorylated intermediate in substrate-level

phosphorylation, but energised state of coupling membranes

was non-phosphorylated, and an intact membrane was

required to couple electron transfer to ATP synthesis.

CHEMIOSMOTIC HYPOTHESIS





Proposed by Peter Mitchell 1961 and further elaborated 1966





Competing hypotheses

1) Chemical hypothesis (i.e. like substrate-level

phosphorylation)

2) Conformational hypothesis

3) Localised proton hypothesis (variation of chemiosmotic)





Peter Mitchell awarded Nobel Prize in Chemistry in 1978.

QuickTime™ and a

TIFF (LZW) decompressor

are neede d to see this picture.

Mitchell proposed that electron transfer directly produced an

electrochemical gradient of protons across the coupling

membrane that was subsequently used to drive ATP

synthesis. The theory was subsequently adapted and

expanded, principally by Mitchell and his colleague Jennifer

Moyle to account for other membrane-linked energy

dependent functions such as the active transport of solutes

across the membrane.

The chemiosmotic hypothesis is named because it is

postulated to involve both

a) chemical reactions, the transfer of chemical groups

(electrons,protons and O22-) within the membrane

b) osmotic reactions, the transport of a solute (protons)

across the membrane

Transmembrane Proton gradient

Energy transduction occurs via a proton circuit which circulates through the

insulating coupling membrane and the two adjacent bulk phases ( the

matrix and the cytosol/ intermembrane space in mitochondria).

Since each of the two bulk phases is in equilibrium, energy storage is

transmembrane rather than intramembrane (intramembrane proton

gradients were the basis of the localised proton hypothesis).

This energy storage takes the form of a delocalised electrochemical

potential difference of protons (H+), otherwise known as the

protonmotive force (p.m.f. or p). It is an electrochemical gradient

because it is composed of both

A chemical potential difference

 pH ( pHout-pHin )

An electrical potential difference or membrane potential



These two contribute to p according to the following relationship

p =  - Z  pH

where Z= 2.303RT

F

R= gas constant, T= absolute temperature in Kelvin, F= Faraday



Z constant approximately equal to 60 at 25oC and serves to convert pH

into electrical units, mV.

ESSENTIAL REQUIREMENTS OF THE CHEMIOSMOTIC

HYPOTHESIS





MITHCHELL PROPOSED THREE ESSENTIAL

REQUIREMENTS THAT HAD TO BE VERIFIED

EXPERIMENTALLY BEFORE THE CHEMIOSMOTIC

HYPOTHESIS COULD BE ACCEPTED AS PROVEN.

Mitchell’s three essential requirements

1) That the respiratory chain redox system (electron transfer)

translocates protons across the membrane in one direction

(anisotropic,direction-oriented) as electrons flow down the

chain.

2) The coupling membrane should be impermeable to

protons and other ions except via specific exchange-diffusion

systems which are involved in active solute transport

3) That the ATP synthase can transport protons across the

membrane in one direction down the concentration ( pH )

and charge ( ) gradient , using the energy for ATP

synthesis. Alternatively it should be able to use the energy

from ATP hydrolysis to pump protons in the opposite direction

(active transport against the concentration and charge

gradient).

Only central part of Mitchell’s hypothesis accepted, that an

electrochemical gradient of protons was both necessary

and sufficient for ATP synthesis linked to electron

transfer.

Specific mechanisms he proposed for proton pumping were

only partially correct, and his chemiosmotic mechanism for

ATP synthase was wrong (this actually involves

conformational change in ATP synthase caused by p.m.f.,

and was partly elucidated as a result of part of the structure

of the ATP synthase being solved by John Walker at

Cambridge, who also received the Nobel Prize).

Was convincing evidence by 1960 that the transfer of energy

via this membrane energised state between the respiratory

electron transfer chain, the synthesis of ATP and the various

solute transfer systems is both efficient and fully

reversible.

Transmembrane Proton gradient

Energy transduction occurs via a proton circuit which circulates through the

insulating coupling membrane and the two adjacent bulk phases ( the

matrix and the cytosol/ intermembrane space in mitochondria).

Since each of the two bulk phases is in equilibrium, energy storage is

transmembrane rather than intramembrane (intramembrane proton

gradients were the basis of the localised proton hypothesis).

This energy storage takes the form of a delocalised electrochemical

potential difference of protons (H+), otherwise known as the

protonmotive force (p.m.f. or p). It is an electrochemical gradient

because it is composed of both

A chemical potential difference

 pH ( pHout-pHin )

An electrical potential difference or membrane potential



These two contribute to p according to the following relationship

p =  - Z  pH

where Z= 2.303RT

F

R= gas constant, T= absolute temperature in Kelvin, F= Faraday



Z constant approximately equal to 60 at 25oC and serves to convert pH

into electrical units, mV.

Mitchell’s three essential requirements

1) That the respiratory chain redox system (electron transfer)

translocates protons across the membrane in one direction

(anisotropic,direction-oriented) as electrons flow down the

chain.

2) The coupling membrane should be impermeable to

protons and other ions except via specific exchange-diffusion

systems which are involved in active solute transport

3) That the ATP synthase can transport protons across the

membrane in one direction down the concentration ( pH )

and charge ( ) gradient , using the energy for ATP

synthesis. Alternatively it should be able to use the energy

from ATP hydrolysis to pump protons in the opposite direction

(active transport against the concentration and charge

gradient).

ATP synthase can transport protons across the membrane in

one direction down the concentration ( pH ) and charge

( ) gradient , using the energy for ATP synthesis.

Alternatively the ATP synthase should be able to use the

energy from ATP hydrolysis to pump protons in the opposite

direction (active transport against the concentration and

charge gradient).

Only central part of Mitchell’s hypothesis accepted, that an

electrochemical gradient of protons was both neccesary

and sufficient for ATP synthesis linked to electron

transfer.

Specific mechanisms he proposed for proton pumping were

only partially correct,

and his chemiosmotic mechanism for ATP synthase was

wrong (this actually involves conformational change in ATP

synthase caused by p.m.f., and was partly elucidated as a

result of part of the structure of the ATP synthase being

solved by John Walker at Cambridge, who also received the

Nobel Prize).

EVIDENCE FOR FIRST REQUIREMENT



1. That the respiratory chain redox system (electron

transfer) translocates protons across the membrane in

one direction (anisotropic,direction-oriented) as electrons

flow down the chain. i.e "An anisotropic proton-

translocating respiratory electron transfer chain"



YOU CAN ONLY MEASURE THE INITIAL EJECTION OF

PROTONS FROM MITOCHONDRIA AS ELECTRON

TRANSFER STARTS, BEFORE THE RE-ENTRY OF

PROTONS HAS BECOME ESTABLISHED. BY

DEFINITION DURING STEADY STATE ELECTRON

TRANSFER THE RATE AT WHICH PROTONS ARE

PUMPED OUT OF MITOCHONDRIA EQUALS THE

RATE OF THEIR RE-ENTRY.

Precautions

)incubate mitochondria anaerobically so no electron transfer

)in lightly-buffered medium so pH/[H+] changes can be observed

)add oligomycin to inhibit proton re-entry via the ATP synthase

)add valinomycin ( a potassium ionophore ) and a high concentration of

KCl to abolish  and thus maximise pH.

)add a small non-saturating pulse of oxygen to start electron

transfer and measure the extent of proton extrusion into the

medium surrounding the mitochondria.

RESULTS

FACTORS CONTRIBUTING TO DECAY OF pH









Protons decay back in to mitochondria across IMM because of

1] inherent proton permeability of IMM – note that FCCP

accelerates the decay

2] action of endogeneous Na+/H+ antiport

3] electroneutral PO4 entry

EVIDENCE FOR SECOND REQUIREMENT

2) The coupling membrane should be impermeable to

protons and other ions except via specific exchange-diffusion

systems which are involved in active solute transport.

It can be deduced that the inner mitochondrial membrane

has a low effective proton conductance by studying the

action of uncouplers. A majority of uncouplers act by

increasing the effective proton conductance of the coupling

membrane, dissipating the proton motive force and thus

breaking the link between electron transfer and ATP

synthesis. It is reasonable to assume that the coupling

membrane has a low proton conductance in their absence.

MECHANISM OF ACTION OF UNCOUPLERS (i.e. FCCP)

Uncouplers are lipophilic (membrane-permeable) weak acids

that can cross the membrane in either the protonated or

deprotonated form. So they act as proton translocators,

catalysing a proton uniport across the coupling membrane.

Driven by  pH









Driven by 

Subsequently Mithchell and Moyle measured the effective

proton conductance of the inner mitochondrial membrane.

This effective proton conductance is one million times less

than that of the surrounding aqueous phases.

i.e. CmH+ < or = 0.5µmho cm-2

Or 0.2 nmol H+ min-1 mg protein-1 mV p-1

EVIDENCE FOR THIRD REQUIREMENT

3) That the ATP synthase can transport protons across the

membrane in one direction down the concentration ( pH )

and charge ( ) gradient , using the energy for ATP

synthesis. Alternatively it should be able to use the energy

from ATP hydrolysis to pump protons in the opposite direction

(active transport against the concentration and charge

gradient) i.e. "A reversible proton-translocating ATP synthase"

EVIDENCE FOR THIRD REQUIREMENT (CONT.)

a)Mitchell and Moyle showed that if you injected a small

amount of ATP into a suspension of anaerobic ( so no

electron transfer) mitochondria there was an expulsion of

protons as ATP was hydrolysed.

b)In mitochondria need to impose a artificial  across the

inner mitochondrial membrane, as active solute transport

uses up pH, so mitochondria work on  for ATP

synthesis. Finally achieved in early 1970's.

EVIDENCE FOR THIRD REQUIREMENT (CONT.)

First demonstration of artificial pH driving ATP synthesis was in 1966 by

Jagendorf and Uribe, using thylakoid membranes of chloroplasts which

don't have solute transport and normally work on high pH and low .

[see handout]

EVIDENCE FOR THIRD REQUIREMENT (CONT.)

First demonstration of artificial pH driving ATP synthesis was in 1966 by

Jagendorf and Uribe, using thylakoid membranes of chloroplasts which

don't have solute transport and normally work on high pH and low .

[see handout]

OTHER EVIDENCE FOR MITCHELL’S CHEMIOSMOTIC

HYPOTHESIS



Related docs
Other docs by qinmei liao
Q CMA ExperienceRequirement
Views: 0  |  Downloads: 0
Lipid Learning Activity
Views: 0  |  Downloads: 0
MATERIAL SAFETY AND DATA SHEETS
Views: 2  |  Downloads: 0
Financial Planning The Ties That Bind
Views: 0  |  Downloads: 0
Inflammatory Pain
Views: 4  |  Downloads: 0
Group goal setting workshop
Views: 0  |  Downloads: 0
MEETINGS REPORT ACTION SHEET
Views: 1  |  Downloads: 0
LYMPHOMA RESEARCH FOUNDATION
Views: 0  |  Downloads: 0
By registering with docstoc.com you agree to our
privacy policy

You are almost ready to download!

You are almost ready to download!