Purple Photosynthesis L10 Flashcards

1
Q

What is the difference b/w chlorophyll a and b and c

A

a and b have a phytyl side chain which make it lipid soluble
c lacks this phytol side chain
Chlorophyll is a substituted tetrapyrrole. The 4 pyrrole nitrogens coordinate a magnesium atom -magnesium porphyrin
The molecule has an extensive system of CONJUGATED DOUBLE BONDS. Electrons are delocalised over this system in molecular orbitals.

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2
Q

Name some light harvesting pigments

A

Carotenoids-linear polyenes, sometimes with one or two cyclic ends, -examples are beta carotene and spheroidenone
Bilins-linear tetrapyrrole that enable cyanobacteria and red algae to utilise YELLOW and GREEN light, -examples are phycocyanin and phycoerythrin

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3
Q

What is the photosystem design?

A

Antennae/light harvesting pigments surround a reaction centre and these collect light energy and pass the energy by RESONANCE transfer to the reaction centre where the ELECTRON transfer happens.
Once the excited state energy is funnelled by resonance energy transfer to the chlorophyll species inside the reaction centre that catalyses the photo-chemical reaction.
Once it arrives at the ‘primary donor’ a chlorophyll species, inside the reaction centre, the excited state energy triggers the PHOTO OXIDATION reaction-producing electron transfer

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4
Q

What is in the reaction centre? And what is in the antenna?

A

Rxn centre-proteins/chlorophylls/quinones/redox centres

Antenna-proteins/light harvesting or antenna pigments/chlorophylls/carotenoids

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5
Q

Resonance energy transfer

A

The Resonance energy transfer of an excited electron is passed to a neighbouring chlorophyll fuelling of energy towards the reaction centre, chlorophylls are activated because energy is passed progressively to RED SHIFT PIGMENTS

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6
Q

Anoxygenic photosynthetic bacteria

A

The most heavily studied are purple non-sulphur bacteria
These do not produce oxygen as a waste product of photosynthesis
CYCLIC electron transfer process, no water oxidation, no oxygen produced
Proteins inside these organisms are very oxygen sensitive

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7
Q

Rhodobacter are metabolically flexible organisms and grow through photosynthesis/anaerobic respiration/aerobic respiration. What colour are they in the absence and presence of oxygen?

A

In oxygen=bright red
anaerobically=brown/green
Their colour comes form the carotenoids not the chlorophyll pigments

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8
Q

The reaction centre in Rhodobacter is similar to PSII. What is it composed of?

A

3 polypeptide chains H L M
H is a single memb spanning helix sits on top of the other two polypeptides in the structure
L is composed of 5 TMS helices
pseudosymmetry to central part of structures in M
M is composed of 5 TMS helices

Structures purpose=structural support/scaffold for the pigment molecules that can either absorb light energy or move electrons around

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9
Q

Structure of Rhodobacter reaction centre

A
4 chlorophyll P870
2 bacteriopheophytins
2 ubiqinones
1 iron atom
1 carotenoid (long linear polyene)

Bacteriopheophytins-speciallised bacteriochlorophyll
no central metal (chlorophylls contain central Mg)
2 protons instead
free acid
TWO BRANCHES arranged around 2 fold symmetry (A=ACTIVE BRANCH)
NB/ ubiquinones and bacteriochlorophylls all have long hydrocarbon tails which make them lipid-soluble

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10
Q

Excitation of the rhodobacter energy

A

p870+ is reduced by by cytochrome c2 (water soluble) cytochrome docks onto the protein surface on the rxn centre and delivers an electron to reduce the cation.
Electron on QA moves laterally in the memb and arrives on the QB quinone. The system has been reset

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11
Q

Ubiquinol formation at QB

A

Double reduction of the UQ at QB is accompanied by the uptake of 2 protons to form ubiquinol. UQH2

Quinones can be either 1 electron redox carrier (if bound to a proton complex interior) or 2 electron/2 hydrogen carriers if its soluble-when free to interchange with the intermembrane quinone pool
Protons do not move across the memb as protons, they move across as hydrogen atoms connected to a quinone molecule-therefore this system is carrying electrons as hydrogen atoms

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12
Q

In photosynthetic bacteria where is proton uptake?

A

Proton uptake occurs in the cytoplasm and release in the periplasm
This generates a proton gradient
Free energy associated with the proton gradient drives protons back through ATP synthase to generate ATP
When ATP is hydrolysed you get lots of free energy out
Energy is locked up in a photon is stored in a high concentration of ATP

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13
Q

In purple bacteria what is the peripheral antenna complex like?

A

LH2 antenna complex consists of concentric cylinders of alpha and beta polypeptides that each have a single transmembrane alpha helix
Eg Rhd sphaeroides LH2 is similar=9 pairs of alpha and beta polypeptides
18 B850 arranged perpendicular to plane of the memb.
9 B800 BChls (rings) -higher energy are arranged parallel to the memb

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14
Q

In purple bacteria what is the core antenna complex like?

A

The core LH1 antenna complex has similar structure to LH2
It is larger so it can surround the reaction centre
Sandwiched b/w 15 pairs of alpha and beta polypeptides is a ring of 32 875nm-absorbing BChls arranged perpendicular to the plane of the memb

BChls in the reaction centre are P870

Energy is funnelled to the reaction centre because LH1 BChls absorb at lower energy than the LH2 BChls
Drop in energy ensures the energy is funnelled in the direction nature needs it to go in, Energetically favourable process.
Size of energy gap gets progressively smaller as you go more RED SHIFTED (longer wavelength)

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15
Q

What makes ubiqinones and bacteriochlorophylls lipid soluble?

A

They have long Hydrocarbon tails

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16
Q

Reaction centre

A

The rxn centre potential difference is coupled to an external circuit
Electron potential difference arises b/w the 2 poles (+p870 -QA)
Used to drive useful external work
Drives subsequent electron transfer in the system

17
Q

What reduces P870+ ?

A

cytochrome c2 (water soluble)
cyt c2 docks onto protein surface of rxn centre and gives an electron to reduce p870+ cation
electron on QA- moves laterally in the memb and arrives at QB quinone
(QB is reduced by QA-)
SYSTEM HAS BEEN RESET

18
Q

Photosystem I

2 active sites connected by an ETC

It is an enzyme with 2 enzymatic activities:
Plastocyanin oxidation
Ferredoxin reduction

Plastocyanin:ferredoxin oxidoreductase

A

Protein in the membrane is trimeric-11 polypeptide subunits (many with multiple TM spanning regions)
100 Chl a
2 phylloquinones
3 Fe4S4 clusters
Carotenoids (127 cofactors in each monomer)

PsaA/PsaB -11 TM alpha helices (Cterminus-5/11TM helices) (heart of complex) PsaC (sticks out of memb) polypeptides bind the cofactors involved in the ETC, forming a rxn centre

PsaA/B N terminus=antenna (6/11 TM helices)
Each bind up to 45 core anntenna chlorophophylls
These domains show homologies to the CP43/47 core antenna complex of PSII

19
Q

Purple Bacteria

A

LH1 and LH2 are packed closely together since need to move E through system relatively rapidly to get it into the rxn centre from where it is initially absorbed.
All pigments have an intrinsic fluorescence life time
Absorb the photon and after a particular moment in time they will emit that photon as fluorescence unless you do something with the energy.

Carotenoids are present in these structures too.

20
Q

Differences b/w PSII and bacterial rxn centre

A

PSII is similar but much larger
It is DIMERIC
At heart of system: reaction centre, CORE antennae, ETC

21
Q

PSII reaction centre

studied more in cyanobacteria than plants

A

Main subunits=D1 and D2 polypeptides
5TM alpha helices

D1/D2 heterodimer similar structure to L/M heterodimer in purple bacteria rxn centre
10 TM alpha-helices 2 fold symmetry axis

4 chlorophylls (2 demethylated Chls in middle of the membrane like the bacterial system)
2pheophytins
bound at interface of D1/D2 polypeptides
2 extra chlorophylls bound in periphery of D1/D2 structure
Mn cluster
2x Tyrosine (Yz/YD)
P680 not P870(bacteria)

33,23,17kDa proteins form oxygen evolving complex and stabilise Mn cluster

22
Q

What is the Mn composed of?

A

Mn complex with Ca and O2 to which water binds

23
Q

Why are plants green?

A

P680 from PSII is in the red part of the spectrum and this is why plants are green-they are full of this red absorbing chl.

24
Q

How is the P680+ cation re reduced in PSII of plants?

A

Re-reduced by electrons delivered via a redox active tyrosine (Yz) from TWO water molecules bound to a cluster of 4Mn atoms and 1Calcium
Yz has high oxidising potential
Redox active
Can lose an electron and pick one up from a donor
Yz+ is sufficiently oxidising to pull an electron off a water molecule bound to the Mn cluster
The Mn cluster catalyses the oxidation of water (pulls FOUR electrons off 2 water molecules) generating molecular oxygen and releasing 4H+

25
Q

Formation of one molecule of water

A

Requires 4 photons with 2PQ reduced to PQH2 and 4H+ taken up (on other side of membrane 2H2O—>O2 + 4H+)

26
Q

Mn/Ca/H2O cluster in PSII plants-how many cycles of oxidation occur?

A

5
(So to S4)
Mn in +3/+4/+5 redox states.

27
Q

What CORE antenna are involved in the PSII system of plants?

A

In the rxn centre (D1/D2) complex is associated with core antenna of the CP43/47 proteins (Chl proteins)
These proteins harvest light energy and feed the E into the p680 Chl species in the rxn centre.

28
Q

Antenna:CP43/47 proteins (Chl proteins)

PSII plants

A

Both have 6TM alpha helices arranged as a TRIMER OF DIMERS and bind a bunch of different Chl/carotenoid molecules.
15 chlorophylls, Beta carotene and lutein (carotenoids)

29
Q

In higher plants and green algae what does the peripheral antenna LHCII consist of?

A

Six types of related integral membrane pigment proteins
Lhcb1-6
Simple structure=trimeric, 3TM helices (1 is DIAGONAL in the membrane-binds a bunch of pigments)
All have highly conserved TM helices and bind varying amounts of Chl a and b, beta carotene, lutein and xanthophyll carotenoids

Excitation energy is transferred from LHCII to the PSII reaction centre via the CP43/47

NB/ xanthophyll pigments are involved in quenching and protection against photo damage (repair)

30
Q

Primary electron donors in PSII and PSI

A

PSII-single chl P680
PSI-dimer chl a P700
bacteria-2chls non covalently attached P870

31
Q

QUINONES what types in Mitochondria/PSII/PSI?

A

Mitochondria-ubiquinone
PSII-plastoquinone
PSI-phylloquinone

32
Q

Ferredoxin

A

Water soluble iron-sulfur protein

33
Q

PSI antennae

plants

A

Has equivalent core antennae to PSII CP43/47
N terminal PsaA/B
binds up to 45 Chls and 10 carotenoids
6/11 TM domains

Peripheral antenna LHCI made of 4 types of light harvesting protein named lhca1-4
like in PSII LHCII lhcb1-6

34
Q

What is the overall photosynthesis eqn in a plant?

A

2H2O + 8photons + 2NADP+ —-> 2 NADPH + O2 + protons translocated

35
Q

What is the issue with PSI and the redox potentials?

How is it overcome?

A

The terminal electron donor, water has more oxidising potential than the terminal electron acceptor, NADP+
(+0.82V) (+0.32V)
electrons want to flow from -ve potentials to +ve potentials

This requires 2 ENERGY INPUT steps using SOLAR power. to generate a more reducing redox potential-the Z scheme!
Pumping energy steps are from the exitation energy from the antenna to form P680+ and P700+ cations/excited singlet state
Causes these complexes to become far more reducing

36
Q

What is the Z scheme? How many volts are the P complexes shunted more negative to give it more appropriate reducing potential? PSII/PSI

A

1.8V

37
Q

How many volts are there in an 870nm photon?

A

1.45V

38
Q

Cyclic and non-cyclic photophosphorylation

A

PSI-participates in both

PSII-non cyclic only