PHOTOSYNTHES

IS AND
PHOTORESPIRAT
ION
Dr M.S. Mafa
Antenna pigments and their associated proteins form light-
harvesting complexes in the thylakoid membrane
 In green plants the reaction center chlorophyll is always chlorophyll-a

 Reaction center pigments present a small target for excitation by an incoming photon

 While the remainder of Chl-a and other pigments are found in the LHC

 Which functions to capture light (photon)

 LHC is made of chl-a, chl-b and carotenoids

 Chl-a, and Chl-b absorbs light at 660-670 nm and 640-650 nm, respectively.

 NB: maximum absorption of chlorophylls associated with proteins of LHCs are shifted toward the red-light

 Thus, LHCs funnel the light towards the reaction centers which traps the energy

 These pigments are attached to proteins in the LHCs (PSII and PSI are associated with LHC-II and LCH-I)

 Generally, LHC contains the chlorophyll :carotenoids in a ratio of about 2:1

Photosystem II and the oxygen-evolving complex

 PSII is one of the two photosystems found in the photosynthesizing organisms

 It function as a water-plastoquinone oxidoreductase

 PSII antenna consists of multiple light –harvesting units

 Four types build from combination of six different chlorophyll a/b binding proteins

 PSII is associated with oxygen-evolving complex

 Oxygen-evolving complex

 Is a site that splits water and provides electrons and protons for initiation of electron transport chain and ATP synthase.
 PSII reaction center is an integral membrane multiprotein complex
containing P680 and electron transport components
 Each PSII reaction center contain two pheophytin molecules

 An ion (Fe) atom

 Two plastoquinone (QA and QB)

 The plastoquinone is the first stable electron acceptor

 Also, P680, pheophytin and plastoquinone are the prosthetic group of the two major reaction center protein D1 and

D2

 D1 is exposed to the extremely oxidizing environment created by excited P680

 This leads to a high rate of D1 breakdown and simultaneous replacement by newly synthesize protein.

 D2, is a 34kDa protein represent the in active branch of reaction center

 CP43 and CP47 are hydrophobic chlorophyll a-binding protein associated with PSII reaction centers
Light-harvesting antenna complex of PSII accounts for half of total
thylakoid protein
 Antenna complex of PSII consists of multiple LHC units

 At least 4-types LHC are build from chl-a and chl-b binding proteins

 LHC-II accounts for 50% of the total protein in plants chloroplast membrane

 LHC-II is a trimer and bind half of the all-chlorophyll molecules in the chloroplast

 Monomers LHC-II contain polypeptide of 230-250 amino acid residue (24-29 kDa)

 It is non-covalently bound to the chlorophyll a, b and two molecules of lutein (see Figure 9.11A above)

 The xanthophyll lutein form a distinctive X-shape

 Xanthophyll function as effective accessory light-harvesting pigment

 It absorb light in a blue and green region

Oxidation of water and reduction of PSII electron acceptors
requires four photons per molecule of oxygen released
 PSII removes electrons from water and passes them to plastoquinone

 Oxygen evolving complex is associated with PSII

 It splits water molecules and donates electrons to PSII

 Light-induced charge separation in the PSII reaction center produces

The S-cycle

P680+
 P680+ is oxidant strong enough to support the endergonic transfer of

electrons from water and the release of oxygen

 four electrons are transferred for every molecule of oxygen produced

 oxygen-evolving transfer electrons to the Mn then Z (tyrosine

residue) of D1 proteins

 Four electrons are produced per one O2 molecules produced; and

protons (S-cycle)
Plastoquinone is the first stable acceptor of electrons from PSII
Electron transport through the cytochrome-b6f complex

 Cytochrome b6f is a plastoquinone-plastocynine oxidoreductase

 It is highly responsive to growth condition and the developmental state of the plant

 The cytochrome b6f complex includes three electron carriers and a quinone-binding protein

 Cytbf structure is highly conserved in all photosynthetic organisms

 It is embedded in the thylakoid membrane as a dimer (220 kDa)

 The monomeric subunit consists of eight subunits

 Four redox components (17-32 kDa)

 Four small polypeptides (smaller than 4 kDa) with an unknow function

 These components are arranged into 13 helices that are embedded into a membrane and extent to lumen
 Cytochrome f component consists of 32 kDa protein- helical-

extending into the lumen

 Cytochrome b6 is 24 kDa

 it has four membrane spanning helices and non-covalently bind to

two b-type heme

 The third redox-active subunit of the Cytb6f complex is a 19 kDa

Figure 9.16B
polypeptide located in the lumen and bound to the thylakoid
 The Rieske iron-sulfur center is bound to the redox-active

protein

 Cytb6f complex also include a quinone- binding 17 kDa protein

called subunit IV

 Then lastly the small proteins with unclear functions but are

important for the assembly of the Cytb6f complex

 Pet G, pet L, pet M, and pet N
Cytochrome b6f complex generates a proton gradient through the
operation of a Q cycle
 The e- moves along an electrochemical gradient from plastoquinone to plastocyanin via Rieske [Fe 2-S2] and
cytochrome f
PHOTOSYSTEM I AND THE FORMATION OF NADPH
 PSI consists of 16 protein subunits arranged in 45 transmembrane helices
 168 chlorophyll molecules
 Three [Fe4 –S4] cluster
 Two phylloquinone or vitamin-1
 The chlorophyll-a, phylloquinone and [Fe4-S4] are electron carriers

 PSI reaction center is called P700

 PSI is largely confined to the inter-granal region of the thylakoid membrane

 PSI reaction center subunits are associated with plastocyanin docking, P700 and
primary and secondary electron acceptors
 It accept e- from plastocyanin and donates them to ferredoxin (Fd)
 The photoexcitation of P700 in the PSI reaction center oxidizes reduced plastocyanin
 P700 transfer e- to first stable acceptor Fx via chlorophyll-a and phylloquinone
 Secondary electron acceptors Fa AND FB are [Fe4-S4]

 Fd accept electrons from FB in turns reduces NADP+ to

NADPH2 via a reaction catalyzed by ferredoxin-NADP+
reductase (FNR)
Photophosphorylation
 Electron transport from PSI to NADPH is an
exergonic reaction
 and its energy is used in chemiosmotic ATP synthesis

 Z-scheme/ non-cyclic e- transport

 Products: O2, NADPH, ATP

 Electrochemical gradient
 Proton accumulation in lumen
 Stroma: ATP synthesis (ATP synthase/ coupling
factor, CF).
 1-1.5 ATP.
ATP is the sole product of cyclic electron flow around PSI
 Additional pathway.

 No water splitting or NADPH formation.

 No PSII.

 Redirects electrons back to cytbf complex.

 Only ATP formation

 Fdred  cytb6f  Q cycle pumps protons into the

lumen  electron to PC  P700+

 cyclic electron flow is regulated by NAD(P)H

dehydrogenase (NDH) and PGR5

CF0-CF1 is a multiprotein ATP synthase complex that uses the proton
gradient across the thylakoid membrane to phosphorylate ADP
 The phosphorylation of ADP to form ATP is catalyzed by the α- and β-

subunits
 in a three-stage binding change mechanism involving the operation

of a proton-driven ‘molecular motor’

 The δ-subunit and subunits I, II and IV function in binding CF1 to CF0,

and subunit III is involved in proton translocation

 ε-subunit and γ-subunit regulate the ATP synthesis during the light

period

 The both inhibit ATP synthesis in the dark