Something Cool
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SOMETHING COOLCH339K
Wooly Mammoth – Mammuthus primigenius
• Disappeared about 10,000 BC• Frozen remains found periodically• Wooly mammoth hemoglobin reconstructed• Campbell, K.L. et al.(2010) Nature Genetics Advance Online
Publication
Structure
• Asian elephant (left) and mammoth (right) deoxyhemoglobin with BPG (chimeric molecule)
• Blue = location of mammoth mutations• Yellow = positive residues on b-chain
Typical hemoglobin
Increasing temperature shifts binding to right
Blood entering warm, exercising muscles unloads more O2.
O2 Binding Curves: Mammoth vs. Asian Elephant
• Intrinsic O2 affinity of mammoth Hb is 2 that of modern elephant
• In the presence of normal cofactors, the two are essentially identical• Increased cofactor affinity, however, reduces temp effects on O2 binding
• Mammoth Hb spec\ialized to deliver O2 to tissues whether cold or hot• Same adaptation seen in reindeer, musk oxen
PHOTOSYNTHESISCH339K
6CO2 + 6 O2 ⇄ C6H12O6
• Requires energy (big surprise)• Provided by radiation• 1017 kcal/year (1010 tons of
carbohydrate produced - 2 tons/person)
Chloroplasts will reduce an artificial electron acceptor when illuminated
Hill Reaction
hE Where h = 6.626 x 10-34 Jsec
And n = frequency (NOT wavelength)
For cyan-colored light, this works out to ~ 240 kJ/mol photons
Absorption of light
• Internal conversion - electronic energy converted to heat, time frame < 10-11 s
• Fluorescence - excited state decays to ground state by emitting photon, time frame ~10-8 s
• Exciton transfer (resonance energy transfer) – excited molecule transfers its excitation energy to nearby unexcited molecules, important in funneling light energy to photosynthetic reaction centers
• Photooxidation - light-excited donor molecule transfers an electron to an acceptor molecule, the oxidized donor relaxes to ground state by oxidizing some other molecule
Chlorophyll is assembled in light harvesting complexesExample shown contains
Chlorophyll A (green)Chlorophyll B (red)Lutein (yellow)
Chlorophylls and accessory pigments harvest incoming photons and are excited
Energy is passed on through exciton transfer to a reaction center
Need 2 e- to reduce the quinone
Pheo = pheophytinQ = quinone
Rhodospirillum action center1) Excited chlorophyll passes electron to pheophytin2) Electron then passed to menaquinone3) Electron passed through Fe to ubiquinone QB 4) Cytochrome donates electron back to action center chlorophyll
Green sulfur bacteria also have a non-cyclic system that passes electrons through ferridoxin to NADPHFerridoxin is an iron-sulfur proteinBelow is ferridoxin 1 from AzotobacterContains one [4Fe-4S] cluster and one [3Fe-4S] cluster
Energetics
Need 2 ferredoxins
Produces good reductant (Ch*) and strong oxidant (Z)
Organization of Photosystem 1
Cytochrome b6f Complex
• Proton pump• Transfers electrons to Plastocyanin (carrier to PS1)• As is complex 3 of ETC, electrons from QH2 have to cycle through one at a
time
Ubiquinone
Plastoquinone
To fix 1 CO2 requires: 2 NADPH molecules 3 ATP molecules
• Each molecule of oxygen released by the light reactions supplies the 4 electrons needed to make 2 NADPH molecules.
• 4 electrons passingthrough cytochrome b6/f complex provides enough energy to pump 12 protons into the interior of the thylakoid.
• To make 3 molecules of ATP, the ATPase in chloroplasts needs about 14 protons (H+)
Deficit is made up by cyclic photophosphorylation. • Electrons expelled by the energy of light absorbed by photosystem I pass, as
normal, to ferredoxin (Fd). • Then pass to plastoquinone (PQ) and on back into the cytochrome b6/f
complex. • Here each electron liberates pumps 2 protons (H+) into the interior of the
thylakoid — enough to make up the deficit left by noncyclic photophosphorylation.
Cyclic Photophosphorylation
Splitting Water
Complex associated with PS II uses several Mn ions to extract 4 electrons from 2 water molecules.P680 is rereduced by Tyrosine in the PSII reaction centerTyrosine radical is rerreduced by increasing oxidation state of a Mn clusterWhen Mn cluster reaches +4 state, it can grab 4 e- from 2 H2O
e- source for PS II