energy metabolism Flashcards
chemiosmotic hypothesis
Coupling of phosphorylation to electron and hydrogen transfer by a chemiosmotic mechanism
proton motive force
proton electrochemical gradient ^p
defined by 2 factors:
proton gradient ^pH
membrane potential ^psi
different types of energy transducing membranes
mitochondrial inner membrane
bacterial inner membrane
photosynthetic bacterial membrane
chloroplast inner membrane
morphology of mitochondria energy transducing membranes
matrix is N
inner membrane space is P
morphology of chloroplast energy transducing membranes
light-driven proton pumping from N (stroma) to P (thylakoid lumen)
thylakoid membrane is arranged in stacked folds
morphology of bacterial energy transducing membranes
proton current
flow of protons through a system
respiratory control
the equilibrium between [ADP] and [ATP] or pH can be disturbed to promote the shift of equilibrium in a favourable direction
eqn: observed mass action
[ATP]/[ADP]
when [ATP]/ADP] is at equilibrium it is called
K equilibrium constant
Gibbs energy increases as
[ATP]/[ADP] is further displaced from K
4 stages of eukaryotic aerobic respiration
glycolysis
oxidative decarboxylation of pyruvate > Acetyl CoA
citric acid/krebs cycle
oxidative phosphorylation
morphology of photosynthetic bacterial energy transducing membranes
invaginated cytoplasmic membrane
can pinch of to form chromatophores at high pressures
proton gradient across a membrane establish…
N- (-ve) and P- (+ve) phase compartment
proton gradients are coupled to…
ATP synthesis
7 mitochondrial respiratory proteins (in spatial order)
Complex 1
Complex 2
UQ
Complex 3
Cytochrome C
Complex 4
ATP synthase
redox carriers in mit. ETC
bacterial Complex 2 proper name, structure & function
Succinate/ ubiquinone oxidoreductase
4 subunits: 2 hydrophilic (flavoprotein & iron-sulphur protein), 2 hydrophobic membrane proteins (heme b-containing and ubiquinone binding site)
3D packed as trimer
e- transfer occurs within monomers
bacterial SdhB (hydrophilic) subunit of Complex 2 contains
3 iron sulphur clusters
[2Fe-2S], [4Fe-4S] and [3Fe-4S]
bacterial SdhA (hydrophilic) subunit of Complex 2 contains
covalently attached FAD cofactor and substrate binding site
what is unusual about bacterial Complex 2 SdhB [2Fe-2S] cluster?
coordination with 3 Cys & 1 Asp
ubiquinone binding site of bacterial Complex 2 structure
cleft between SdhB, C & D close to [3Fe-4S]
side chains of Tyr 83 & Trp 164 are direct ligands to ubiquinone
role of heme B in bacterial Complex 2
electron sink for those not passed to UQ
high redox potential attracts e-
close to UQ binding site
structure & function of mitochondrial Complex 2
Two hydrophilic subunits
Flavoprotein (FP)
Iron-sulphur protein (IP)
Two hydrophobic membrane subunits
CybL and CybS, that contain one heme b and provide two ubiquinone binding sites.
name & describe advantage of the 2 mit. UQ binding sites
Qp and Qd
favours the transfer of two electrons from reduced FADH2 to ubiquinones with high efficiency as it increases stability of bound UQ over that increased time period of e- transfer
3 distinct quinone redox carriers across kingdoms
UQ in mitochondria
menaquinone in anaerobic bacteria
plastoquinone in chloroplasts
proper name of Complex 3
Q-cytochrome c oxidoreductase
Q-cycle
coupling of e- transfer from Q > cyt c to transmembrane proton transport
in Q cycle, UQ is reduced to
semi-quinone anion Q-
Q-cycle mechanism summary
2molecules of QH2 are oxidised > 2 molecules of Q.
1 molecule of Q is reduced > QH2.
2 molecules of cytochrome c are reduced.
4 protons are released to the cytoplasmic side.
2 protons are removed from the matrix side.
Q-cycle inhibitors & modes of action
Myxothiazol – blocks reactions at the QP (Qo) site
Antimycin – acts on the QN (Qi) site preventing the formation of the relatively stable UQ.-.
Stigmatellin – inhibits electron transfer to the Rieske protein.
gated control of Complex 3 by Rieske ISP
Reduction of the Rieske centre causes the ISP to move to a new docking position close to cytochrome c1.
after E- > c1, ISP has reduced affinity for c1 heme and moves back > Q site.
ISP is bound to c1 is too far from Qp site to accept e-
so 2nd e- must > bL heme.
Complex 4 proper name
cytochrome c oxidase
5 stages of oxygen reduction in Complex 4
- formation of oxy species
- formation of P species
- formation of F species
- formation of hydroxyl
- condensation
2 proton channels speculated to be responsible for proton pumping
K (conserved aspartate) and D (lysine)
these aminos have their side chains projecting into the respective channels
not found in all mitochondrial and bacterial enzymes
supercomplex
arrangement of ETC proteins into a supramolecular structure that aids e- and proton transfer
redox potential
ability of redox couple to attract e-
negative E0 = lower affinity for e- than standard (more likely to form ions)
positive E0 = higher affinity for e- than standard (less likely to form ions)
what happens when the gain of e- changes the pKa of 1 or more ionizable groups?
reduction is accompanied by gain or 1 or more protons
when NAD+ undergoes 2e- reduction it gains _ protons
1
when UQ undergoes 2e- reduction it gains _ protons
2
when cyt c undergoes 2e- reduction it gains _ protons
0
how do prosthetic groups increase e- transfer speed?
if they are in contact they can act as e- tunnels
usually, the max separation between prosthetic groups forming an e- tunnel is
14 Angstrong
e- flow from centres of _ E0 to centres of _ E0
low > high E0
in what part of complex IV does the biochemistry take place
2 core subunits
ancillary proteins have little/unidentified effect on biochem
which complex IV proton channel is responsible for chemical proton uptake for catalysis
K with conserved lysine
which complex IV proton channel is responsible for proton uptake/pumping for pmf
D for aspartate
bacterial etc location
P = periplasm
N= matrix
ETC proteins embedded in cytoplasmic membrane
bacterial etc differs from mit etc
shorter and more flexible
i.e. no complex 3, all e- are delivered directly to and accepted from quinone pool
Complex IV differences in bacteria compared to mit.
-different structure haem of haem-copper centre
-lower affinity for oxygen, so when [O2] gets too low it switches to a cyt b oxidase with higher O2 affinity and no proton pump
which of the two is membrane embedded: NAP or NAR?
NAR
which of the two is more bioenergetically efficient: NAP or NAR
NAR, uses 2 protons from N to reduce NO3- to NO2-
cofactors, by subunit, of NAR
NarG MGD & [4Fe-4S]
NarH 3x [4Fe-4S] 1x [3Fe-4S]
NarL 2x bis-coord cyt c
cofactors, by subunit, of NAP
NapA MGD-Cys & [4Fe-4S]
NapB 2x bis-coord cyt c
NapC 4x bis-coord cyt c
what pathways occur in chloroplasts?
respiration, photosynthesis, other biosynthetic pathways
amyloplast
plastid specialised for starch synthesis and storage
light independent reactions of photosynthesis name and function
Calvin-Benson-Bassham cycle
fixation of CO2 to make sugars, with help from ATP and NADPH from light dependent reactions
light independent reactions of photosynthesis name and function
light energy harvested to convert NADP+ and ADP > NADPH and ATP
key enzyme of CBB cycle
Rubisco
give the 2 products of photosynthesis
starch & sucrose
how is the electrochemical gradient created in chloroplasts
H+ pumped > thylakoid lumen during e- transport
this is used for ATP synthesis
electron shuttle proteins in thylakoid membranes
plastoquinone and plastocyanin
how is NADP+ reduced in the thylakoid
PSI reduces ferredoxin
reduced Fd will reduce NADP+ with catalysis from ferredoxin-NADP reductase
order of photosynthetic proteins
PSII
b6f
PSI
FNR
F-ATPase
chloroplast assembly/proteins is coded by _ DNA
nuclear and chloroplast
PSII structure
Mn-containing oxygen evolving complex (OEC) held in Mn stabilising protein (MSP)
core: D1 and D2 proteins. D1 tyr is essential for e- transport
various chlorophyll binding proteins
associated with light harvesting complexes (LHC)
what is D1 repair and why is it necessary?
PSII polypeptides, particularly D1 get oxidative damage by P680+ and 1^O2 radicals
Stn8 kinase activated by reduced PQ(H2) pool phosphorylates the damaged polypeptides.
the complex is disassembled (modular structure) and only D1 is resynthesised and integrated back in.
cofactor of ferredoxin-NADP reductase
flavin a.k.a FAD
how is photosynthetic activity tuned to FNR availability?
In the dark at low stromal pH, binding is strong and FNR is sequestered and stabilised on the thylakoids.
In the light, stromal pH increases, releasing FNR to catalyse NADP reduction.
Photon flux density units
umol quanta m-2 s-1
photon flux density/irradiance =
flux of radiant energy per unit area
as irradiance increases, excess light
also increases
other conditions that can increase excess light
stressful conditions that limit CO2 fixation like low temp, drought etc
long term adjustment to light level fluctuations
thickness of leaf, less light = less cells required for photosynthesis, so thinner leaf.
PPFD or photosynthetic photon flux density =
amount of quanta in the photosynthetic range
photosynthetic wavelength range
400-700 nm
leaves grown at higher PPFD have a _ light saturated CO2 assimilation rate because of _
higher
because of thicker leaves through which high light intensity can penetrate and higher [rubisco] and other enzymes in CBB cycle
leaf movement purpose
short term adjustment to gain more light or avoid light
light perceived by blue light absorbing phototropin photoreceptors
chloroplast movement purpose
short term adjustment, directed by cytoskeleton which chloroplasts are tethered to to gain more light or avoid
light perceived by blue light absorbing phototropin photoreceptors
phototropin photoreceptors
absorb blue light
contain flavin cofactor
located outside chloroplast
PHOT1 & PHOT2
coordination between _ and _ is required to adjust to environmental changes
nucleus and chloroplast because they each contain genes for essential protein subunits
2 mechanisms for rapid response to excess energy excitation
- state transitions to balance PSII and PSI excitation
- preventing excitation energy absorbed by LHCs from reaching photosystem reaction centres. excess energy re-radiated as heat via non-photochemical quenching
NPQ mechanism
- photochemistry
- formation of triplet excited chlorophyll
which results in singlet oxygen and photo-oxidative stress - fluorescence emission
- dissipation as heat
triplet excited chlorophyll =
pair of electrons are split between two orbitals of exceeding energy with unpaired spin (spin in same direction)
singlet excited chlorophyll =
pair of electrons are split between two orbitals of exceeding energy with paired spin (spin in opposite directions)
singlet ground chlorophyll =
pair of electrons in same orbital with paired spin (spin in opposite directions)
damage caused by reactive singlet oxygen
damage to thylakoid membrane, particularly reaction centre components
oxidises highly unsaturated fatty acids in membrane producing lipid radicals and hyperoxides
SOSG =
singlet oxygen sensor green
fluorescent probe to visualise singlet oxygen production
SOSG mechanism =
-SOSG > leaves
-becomes fluorescent when oxidised by singlet oxygen
-this form an endoperoxide
measuring NPQ by chlorophyll fluorescence analysis (2 methods)
- illuminate with blue light and measure red fluorescence at wavelength specific to PSII
- illuminate with white light that pulses at fixed frequency and measure PSII red fluorescence emitted at same frequency. (modulated fluorimetry)
extent of fluorescence emission (F) from chlorophyll depends on
photosynthetic activity
i.e. if photochemistry is slow, F increases
or if excitation energy is dissipated by NPQ, F decreases
quantum efficiency
mol O2 produced /mol quanta absorbed
ratios between fluorescence signals can be used to calculate
quantum efficiency
photochemical quenching
non-photochemical quenching
photochemical quenching
estimate of redox state of plastoquinone PSII acceptor
NPQ comprises 3 components
qE
qI
qT
qE =
energy dependent quenching
rapidly reversible
main component (usually)
qI =
photoinhibitory quenching
from inactivation of PSII reaction centres
important in severe excess light
qT =
state transitions
movement of LHCII between PSII (granal stacks) and PSI (unstacked stromal lamellae)
2 components of qE
both activated by acidification of thylakoid lumen as light intensity and H+ pumping increases
1. xanthrophyll cycle
2. PsBs protein
xanthrophyll cycle
VDE (activate by low pH) converts violaxanthin to zeaxanthin
less polar Z associates with LHCs and absorbs excess excitation energy, efficiently radiates this as heat
low light = pH increase, = VDE activity decrease, = Z to V by enzymes
PsbS protein
associates with PSII and LHC to facilitate structural changes when protonated
PsbS protein is not essential for qE but is needed for
rapid response to large light intensity increase
how is NPQ a problem for crop photosynthesis
NPQ takes a long time to relax after high light intensity events
while NPQ is high, CO2 fixation is limited because of decreased e- transfer rate
can fix by increasing ZEP (Z > V) activity
photoprotective role of carotenoids
in algae: absorb excess light before it enters chlorophyll
qT mechanism
PSII gets overexcited so STN7 kinase activates and phosphorylates LHCII
surface charge change induces LHCII movement > PSI
excess excitation of PSI decreases STN7 activity allowing dephosphorylation and movement > PSII
how is excitation imbalance between PSII and PSI sensed to activate STN7
redox state of plastoquinone acts as sensor
activates STN7 when reduced
how can Plastoquinone measure PSII and PSI relative activity
lies between them
PQ redox state controls expression of photosynthesis-associated genes in chloroplast and nucleus
how was cyclic electron transport shown to act as a protectant for PSI in high and fluctuating light intensity
mutation to PGR5 in Arabidopsis causes sensitivity to fluctuation of light intensity
Yamamoto and Shiknai 2019
PGR5 = proton gradient regulating protein
other electron sink proteins/reactions
flavodoxins
flavodiiron proteins
alternative oxidase (AOX)
mehler reaction
flavodoxin mechanism
-alternative low potential PSI e- acceptor in photosynthetic bacteria and algae
-flavin mononucleotide e- carrier (less susceptible to ROS damage than FeS)
-slower turnover
-functional when expressed in plants
flavodiiron mechanism
-additional PSI e- acceptor
-cyanobacteria, algae and vascular non-flowering plants
accpet e- from PSI and reduce O2 to water
-evidence based off mutants
complex I name and general structure
-NADH:ubiquinone oxidoreductase
-membrane embedded arm, periplasmic arm
-periplasmic arm contains Fe-S wire
-membrane embedded arm contains proton pumps, discontinuous helices that form dipoles
-may undergo conformational change to bring UQ binding site close enough for e- transfer from Fe-S
-cage of 30 supernumerary subunits around core units in mammalian cells protect from oxidative damage
-cage does not protect subunit that binds NADH so possibly this is replaced once damaged
complex 1 function
take 2e- from NADH and pass onto UQ
pumps 4H+
what is photoprotection
process of removing excess light energy absorbed by chloroplasts to prevent damage to photosystems and photosynthetic inhibition.
photon flux density
amount of photosynthetically active photons (400-700nm) hitting a surface per unit area per unit time.
umol quanta m-2 s-1
how do leaves grown under high light intensity for long periods of time differ from leaves grown under low light intensity for long periods of time and why?
high intensity = thicker leaves to make use of high incoming light intensity; also exhibit higher CO2 assimilation rate and photosynthesis
lower intensity = thinner and lower CO2 assimilation rate and photosynthesis
how is photosynthetic CO2 assimilation measured
passing air through leaf chamber clipped to leaf surface and measuring the change in [CO2] with an infrared gas analyser
what protein is important for light sensing and photosynthetic efficacy
phototropin senses blue light with a flavin cofactor
PHOT1 & PHOT2
involved in movement of chloroplasts in response to short term light fluctuation
short term adjustments of chloroplasts in response to high and low light intensity
high = chloroplasts move to side of leaves to shade one another and prevent excess excitation energy
low = chloroplasts move to top of leaves to harness as much light energy as possible per chloroplast
mediated by phototropin
phenotypic effect of PHOT2 mutant
leaf cells unable to move chloroplasts and susceptible to photoinhibition
adjustment to prevailing environmental conditions requires… (photosynthesis)
retrograde signalling
what is retrograde signaling
general = signal travels backward from target to original source (signals made from nuclear genome)
specific = co-ordination between expression of photosynthetic genes in chloroplast and nucleus
how does retrograde signaling work and what is the point
- metabolic conditions in chloroplast generate signals
- signals -> nucleus
- signals influence nuclear gene expression
- enables the correct number of photosynthetic machinery to be synthesised and from nuclear genome for use in chloroplasts
2 molecular pathways for rapid response to excess excitation energy
- state transitions to balance PS1 and PS2 excitation
- preventing LHC-absorbed excitation energy from reaching reaction centres by re-radiating it as heat (non-photochemical quenching/NPQ)
alternative fates of excited chlorophyll in LHC
- normal photosythesis
- formation of triplet excited chlorophyll during photosynthesis
triplet excited chlorophyll -> singlet oxygen production and photo-oxidative stress - fluorescence emission
- dissipation as heat
LHC
light harvesting complexes
why is triplet chlorophyll dangerous
interacts with oxygen to form singlet oxygen which is highly electrophilic and causes damage to thylakoid compartment and reaction centre components
- oxidises highly unsaturated fatty acid in thylakoid membrane to produce lipid radicals and hydroperoxides
method of visualising singlet oxygen production
singlet oxygen sensor green
- fluorescent probe which permeates into chlorophyll and reacts specifically to singlet oxygen when produced
- high light increases SOSG oxidation
- DCMU blcoks Qa plastoquinone binding site of PSII and increases SOSG oxidation
why does blocking the Qa binding site of PSII with DCMU increase SOSG oxidation?
- halts electron transfer
- this causes build up of triplet and singlet chlorophyll
how to measure NPQ and why it is done this way
- illuminate with blue light and measure red fluorescence at PSII specific wavelength
- illuminate with white light pulsing at fixed frequency and measure at same PSII specific wavelength
- modulated fluorimetry allows measurements when leaves are photosynthesising under normal illumination
what does red fluorescence in modulated fluorometry of NPQ mean
excited singlet chlorophyll returns to ground state by the emission of red fluorescence
how and why is the Fm signal generated
how
- fluorescence signal emitted after leaves treated with high intensity light flash
why
- enables calculation of Fv/Fm which is proportional to quantum efficiency of photosynthesis
why is Fv/Fm a good measure of the state/ efficiency of photosynthetic apparatus
decreases under conditions that cause damage to photosynthesis
what is the purpose of photochemical quenching
gives an estimate of the redox state of plastoquinone PSII 2e- acceptor and ergo used to estimate photosynthetic e- transfer rate
why do plants grown in lower light intensities emit more chlorophyll fluorescence when exposed to high light
lower photosynthetic capacity so a larger proportion of the incident light is emitted as fluorescence.
these plants also generate higher rates of NPQ
nigericin
- uncoupling agent
- prevents build up of trans-thylakoid membrane pH gradient
- this greatly decreases NPQ when light is on
NPQ is dependent on
development of pH gradient across thylakoid membrane
xanthophyll cycle mechanism
- violaxanthin de-epoxidase (VDE) converts violaxanthin (V) to zeaxanthin (Z)
- VDE activated by low pH, using ascorbic acid as reductant
- less polar zeaxanthin associates with LHCs where it absorbs excitation energy from chlorophyll and efficiently re-radiates it as heat
- In low light, lumen pH increases, VDE activity decreases, and the conversion of Z to V by zeaxanthin epoxidase
PsbS protein mechanism
- associates with PSII and LHC and facilitates structural changes when protonated
how does qE change the structural arrangement of PSII-LHCII and how does this contribute to energy release
- normal pH, V present and LHC in trimers
- when high light present, acidification of thylakoid lumen triggers V->Z, trimers of LHC aggregate
- in aggregated state, excitation energy of chlorophylls excites Z
- Z structure favours the ability to lose excitation energy as heat
what did chlamydomonas carotenoid npq1 and lor1 show?
both pigments requirements for NPQ and survival of cells in high light
mutant npq1 grew okay,
while lor1 didn’t and was pale
double mutant completely bleached by high light
how does NPQ limit rate of photosynthesis during crop production?
time taken for NPQ to relax after exposure to high light
NPQ diverts excitation energy away from photosystem two reaction centre, while it is operating the rate of photosynthesis efficiency of photosynthesis will be lower
how was expedited NPQ relaxation engineered
- speed up the rate of NPQ relaxation by increasing the zeaxanthin epoxidase (ZEP) activity
- removes zeaxanthin more rapidly in low light
- however also necessary to balance the increase in ZEP activity ith violaxanthin de-epoxidase and PsbS expression.
- overall strategy: transgenic plants in which all three proteins expressed at higher level.
how was expedited NPQ relaxation engineered
- speed up the rate of NPQ relaxation by increasing the zeaxanthin epoxidase (ZEP) activity
- removes zeaxanthin more rapidly in low light
- however also necessary to balance the increase in ZEP activity ith violaxanthin de-epoxidase and PsbS expression.
- overall strategy: transgenic plants in which all three proteins expressed at higher level.
- advantage only in naturally fluctuating light, didn’t effect plants grown in labs under constant light intensity
cytoplasmic carotenoids may shield chloroplasts from
excess light
how is balancing of excitation achieved by state transitions?
- PSII is over-excited, protein kinase STN7 is activated and phosphorylates LHCII
- change in surface charge induces LCHII movement to towards PSI
- Excess excitation of PSI decreases STN7 activity allowing dephosphorylation and migration back to PSII
what is the importance of balancing excitation between photosystems via state transitions
If photosystem two becomes overexcited compared to photosystem one there will be an imbalance in electron transport potentially leading to photoinhibition.
favoured hypothesis of state transitions STN7 activation
- redox state of plastoquinone acts as the sensor and activates STN7 when it becomes more reduced.
- plastoquinone (PQ) lies between PSII and PSI so its redox state can measure their relative activity.
key evidence for favoured hypothesis of state transitions STN7 activation
- DCMU blocks electron transport before plastoquinone
- DBMIB blocks electron transport after plastoquinone
- these inhibitors have opposite effects on the redox state of plastoquinone and they affect state transitions correspondingly
how does plastoquinone act as a signal besides during state transition
- acts as a signal to activate gene expression in the nucleus
- proteins involved in longer term acclimation to high light can be synthesised and transported into the chloroplasts
how do arabidopsis mutant studies show cyclic e- transport has a photoprotective role
- pgr5 mutants have increased sensitivity to fluctuating light
- NDH-dependent route involves three distinct NADPH dehydrogenases.
- Knocking out all three of these genes in tobacco causes it to be more sensitive to high temperature disruption of photosynthesis.
- deficiency of pgr5 leads to degradation of photosystem one
4 alternative e- sinks for photosynthetic e- transport
Flavodoxins: flavin mononucleotide- FMN proteins act additionally to ferredoxin. Found in bacteria and some algae but not flowering plants.
Flavodiiron proteins: group of diiron/FMN oxidases. accept electrons from PSI, reducing oxygen to water. Occurs in cyanobacteria, algae, mosses and ferns but not flowering plants.
Mehler reaction: transfer of e- from PSI to oxygen forming hydrogen peroxide. PSI reaction centre may act as e- donor.
Alternative oxidase (AOX): mitochondrial diiron oxidase accepting e- from Complex 1. Reduces oxygen to water, bypassing proton transport and ATP synthesis. strong evidence that leaf mitochondria can oxidise excess reductant exported from chloroplasts and imported into mitochondria as NADH. AOX mutants are susceptible to photoinhibition in chloroplasts. NADH consumption is also aided by activation of uncoupling proteins.
flavodoxin as alternative low potential PSI e- acceptors
- Flavodoxins can act additionally to ferredoxin (2Fe2S) in cyanobacteria, some algal groups and mosses.
- Thought to have evolved in response to Fe deficiency following appearance of oxygen from cyanobacterial photosynthesis.
- Flds contain a flavin mononucleotide (FMN) electron carrier instead of FeS, rendering them less suspectable to damage by oxygen and reactive oxygen species.
- They have a slower turnover than Fd but are functional when expressed in plants, being able to interact with FNR to reduce NADP+.
- Fe deficiency (which is common in the ocean) induces algal Fld, decreasing the Fe requirement for photosynthesis
- Under severe stress Fld can be inactivated by oxidation of the FeS centre and Fe loss. Plants expressing cyanobacterial Fld maintain photosynthesis better under various stresses additionally to Fe deficiency.
flavodiiron proteins provide an additional PSI e- acceptor to ferredoxin
- in bacteria, algae and vascular plants
- evidence they accept electrons from PS1 and reduce oxygen to water.
- Evidence based on mutants in various flavodiiron (Flv) proteins: decreased formation of H218O from supplied 18O2 measured by mass spectrometry; greater reduction of the PSI reaction centre chlorophyll (P700) measured by P700 absorbance.
3 ways antioxidant systems works
- removal of ROS
- prevention of radical formation
- repair damaged molecules
oxidative damage
ROS can result in further reactions that result in production of free radicals and damage to biomolecules
ROS
electronically excited oxygen species
superoxide/hydrogen peroxide + iron sulphur proteins =
release of iron and inactivation
