Ellis Seminar 3:15 pm SL 120

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Ellis Seminar 315 pm SL 120
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Figure 22-42 Energy-dependent binding change
mechanism for ATP synthesis by proton-translocatin
g ATP synthase.
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Synthase Cartoon http//rsb.info.nih.gov/NeuroChem
/biomach/ATPsyn.htmlI
Another animation http//www.res.titech.ac.jp/s
eibutu/
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Figure 22-43 Model of the E. coli F1F0ATPase.
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Figure 22-44a Rotation of the c-ring in E. coli
F1F0ATPase. (a) The experimental system
used to observe the rotation.
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Figure 22-44b Rotation of the c-ring in E. coli
F1F0ATPase. (b) The rotation of a 3.6-?m-long
actin filament in the presence of 5 mM MgATP as
seen in successive video images taken through a
fluorescence microscope.
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Animation http//www.res.titech.ac.jp/seibutu/pro
jects/fig/f1rot_3.mpg Rotation of the gamma
subunit of thermophilic F1-ATPas was observed
directly with an epifluorescent microscope. The
enzyme was immobilized on a coverslip through
His-tag introduced at the N-termini of the beta
subunit. Fluorescently labeled actinfilament was
attached to the gammma subunit for the
observation. Images of therotating particles were
taken with a CCD camera attached to an image
intensifierrecorded on an 8-mm video tape.
(Noji et al. Nature 386 299-302 1997)
Synthase Movie http//www.cnr.berkeley.edu/hongw
ang/Project/ATP_synthase /QT_movies/F1_3d_sp_2.mov
Synthase cartoon http//rsb.info.nih.gov/NeuroChe
m/biomach/ATPsyn.htmlI
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Figure 22-46 Uncoupling of oxidative
phosphorylation.
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CH 23 Gluconeogenisis and Pentose Phosphate
Pathway
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Figure 23-1 Pathways converting
lactate, pyruvate, and citric acid cycle
intermediates to oxaloacetate.
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Figure 23-2 Conversion of pyruvate to
oxaloacetate and then to phosphoenolpyruvate.
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Figure 23-3a Biotin and carboxybiotinylenzyme.
(a) Biotin consists of an imidazoline ring that
is cis-fused to a tetrahydrothiophene ring
bearing a valerate side chain.
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Figure 23-3b Biotin and carboxybiotinylenzyme.
(b) In carboxybiotinylenzyme, N1 of the biotin
ureido group is the carboxylation site.
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Figure 23-4 Two-phase reaction mechanism of
pyruvate carboxylase.
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Figure 23-4 (continued) Two-phase reaction
mechanism of pyruvate carboxylase. Phase II
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Figure 23-5 The PEPCK mechanism.
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Figure 23-6 Transport of PEP and OAA from
the mitochondrion to the cytosol.
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Figure 23-7 Pathways of gluconeogenesis and
glycolysis.
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Table 23-1 Regulators of Gluconeogenic Enzyme
Activity.
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Figure 23-8 Hormonal regulation of F2,6P.
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Figure 23-9 The Cori cycle.
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Figure 23-10 The glyoxylate cycle.
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Figure 23-11 Role of nucleotide sugars.
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Table 23-2 Sugar Nucleotides and Their
Corresponding Monosaccharides in
Glycosyltransferase Reactions.
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Figure 23-21a Chemical structure of tunicamycin.
(a) The structure of the glycosylation
inhibitor tunicamycin.
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Figure 23-22 Chemical structure of bacitracin.
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Figure 23-25 The pentose phosphate pathway.
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Figure 23-26 The glucose-6-phosphate
dehydrogenase reaction.
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Figure 23-27 The phosphogluconate dehydrogenase
reaction.
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Figure 23-28 Ribulose- 5-phosphate isomerase
and ribulose- 5-phosphate epimerase.
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Figure 23-29 Mechanism of transketolase.
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Figure 23-30 Mechanism of transaldolase.
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Figure 23-31 Summary of carbon skeleton
rearrangements in the pentose phosphate pathway.
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