W4 Electron Transport and Oxidative Phosphorylation Flashcards
how are the 12 electron pairs involved in glucose oxidation transferred to O2
transferred to coenzymes NAD+ and FAD > form 10 NADH and 2FADH2 > become oxidised in electron transport chain
anatomy of mitochondria
inner membrane highly to form cristae
heart muscle cells have high rates of respiration > densely packed cristae
liver cells with lower respiration rates > sparsely distributed cristae
electrochemical gradient generated by protons across membrane by complex I, III and IV
what is the malate-aspirate shuttle
electrons in NADH are used to reduce cytosolic oxalacetate into malate > malate transported into mitochondria via malate-alpha-ketoglutarate carrier > oxidised back into oxalacetate to release NADH again
what is the glycerophosphate shuttle
- cytosolic NADH from glycolysis transfers its electrons to DHAP > converted to glycerol-3-phosphate, catalysed by glycerol-3-phosphate dehydrogenase
- glycerol-3-phosphate enters mitochondria > reoxidation of FADH2 with the passage of electrons into the ETC
how does atp-adp translocate mediate movements of atp and adp
has single nucleotide binding site facing matrix > binds to atp > reorients to face inter membrane space > exchange for adp > face back matrix
outside of inner membrane more positive than inside due to pumping of protons > atp more negative than adp > outward movement of atp is favoured
concept of electron transport chain
most of chain’s components are proteins
carriers alternate reduced and oxidised states as they accept and donate electrons
electrons drop in free energy as they go down the chain and pass to final e acceptor, O2, forming H2O
it breaks the large free energy drop from food to O2 into smaller steps that release energy in manageable amounts
what does it mean to have a more positive standard reduction potential
more positive > greater the tendency for the redox couple’s oxidized form to accept electrons and become reduced
how many ATP is produced per oxidation of one NADH
3
structure and function of complex I (NADH dehydrogenase)
consists of about 45 subunits > core structure includes flavin mono nucleotide and several iron-sulfur clusters
NADH donates two electrons to FMN > reduced to FMNH2 > e passed through series of Fe-S clusters in complex > transferred t o coenzyme Q
properties of coenzyme Q (ubiquinone)
a lipophilic EC with benzoquinone linked to an isoprene-containing tail
can transfer two electrons in one electron step via a stable semiquinone intermediate
provides a link between two-electron carriers and one-electron carriers
structure and function of complex II (succinate dehydrogenase)
made up of 4 subunits including FAD and heme, not involved in pumping of protons
catalyse oxidation of succinate to fumarate in TCA > FAD reduced to FADH2
electrons from FADH2 transferred through Fe-S clusters in complex II to coenzyme Q > reduce it to ubiquinol > ubiquinol carries these electrons to complex III
structure and function of complex III (cytochrome bc1 complex)
11 subunits; cytochrome b consisting of 2 heme groups, low and high spin, cytochrome c1 and Fe-S
catalyse transfer of electrons from ubiquinol to cytochrome c in intermembrane space > pumps two protons into IMS for every 2 electrons transferred
about 250kDa and functions as a dimer with each monomer composed of 10 or 11 protein chains
what happens in the Q cycle
first e transfer: ubiquinol donates one e to cytochrome c via Fe-S and another to cytochrome b > reduces a semiquinone at Qi site
second round: another ubiquinol repeats this process > fully reducing semiquinone back to ubiquinol > pump total of 4 protons into inter membrane space
structure and function of cytochrome c
contains a heme group with iron that can alternate between Fe2+ and Fe3+ > transfer electrons from Fe-S of complex III > migrates along membrane surface in reduced state > carry electrons to complex IV (cytochrome c oxidase)
structure and function of complex IV (cytochrome c oxidase)
accept electrons from cytochrome c > transferred through two heme and two copper centers > catalyze reduction of O2 to H2O with the use of 4 electrons from cytochrome c and 4 protons from matrix