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Lecture 4

BIOC 3560 Lecture 4: biochem PACK FOUR.pdf


Department
Biochemistry
Course Code
BIOC 3560
Professor
Marc Coppolino
Lecture
4

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Lectures 5-7
Chapter 5:
- p. 165 - 172
- 5.3 Protein Interactions Modulated by
Chemical Energy p. 179-181; 182-184
problem #7, p. 185
Chapter 6:
- p. 189-203 (review)
- 6.5 Regulatory Enzymes
p. 226-232; 235-236

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Lehninger 6e
Fig. 5-5
Review: In globins, steric hindrance and a H-bond
between His E7 and O2 (thermodynamically
favourable) improve the specificity of binding to O2.
Selectivity is not perfect, however, and CO binds with
higher affinity, but not as high as to free heme
BINDS CO MORE THAN O2, LIMITS ABILITY TO USE O2

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Lehninger 6e Fig. 5-4
pO2
θ =
pO2 + P50
Myoglobin binds O2 with
high affinity, and for a
wide range of pO2 it is
relatively insensitive to
changes in pO2.
At the pO2 of tissues
(~ 4 kPa), it is
nearly saturated.
O2-binding by myoglobin
Showing occupancy
want an O2 transporter
PO2 = partial pressure
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