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Flashcards in Chapter 5 Deck (15):
1

Describe cooperative binding

"Snow ball effect" where binding of one oxygen breaks and reforms bonds, which leads to other heme subunits having a higher affinity for oxygen

2

Pharmacophore

A part of a molecular structure that is responsible for a particular biological or pharmacological interaction that it undergoes

3

Hemoglobin characteristics (6)

-4 heme strucutures
-4 binding sites
-Lower affinity for O2
-Sigmoidal
-Cooperativity
-O2 transport

4

Myoglobin characteristics (6)

-1 heme structure
-High affinity for O2
-No cooperative binding
- O2 bound at any concentration
-Hyperbolic growth
-O2 storage

5

Myoglobin and Hemoglobin similarities

-Ring polythirin
-Chelate Fe2+ in middle of structure
-Proximal and distal histidine
-Globular proteins
-Both bind O2

6

What are the benefits of using protein-heme-iron system vs. free iron for oxygen transport

Free floating Fe2+ would most likely oxidize Fe2+ to ferric Fe3+, which would lose the function to bind to oxygen. Hemoglobin protects Fe2+ and is able to convert Fe3+ back to Fe2+ after it is bound to oxygen

7

Proximal histidine characteristics

-Anchors Fe3+ in heme structure
-Close to heme ring

8

Distal histidine characteristics

-Closer to O2
-Helps protect O2 binding site
-Helps keep CO from binding
-Makes O2 bind at angle

9

T State characteristics (5)

-Low O2 (not bound)
-Starts at tissues, goes to lungs, turns into R state
-Large pocket
-Stable
Inactive/deoxygenated

10

R State characteristics (5)

-High O2
-Starts at lung, goes to tissues, turns into T state
-O2 bound
-Increase O2 affinity
-Small

11

Explain coopertivity in relation hemoglobin

When the first O2 binds to Hb, it interacts with the entire ring by stretching it. This increases the affinity that 2,3,4 subunits have for O2, making it easier for them to be bound to O2. Opposite is true for releasing O2.

12

Coordinate covalent bonds

Four pyro nitrogens donate electrons to Fe2+ group in the middle of hemoglobin

13

Why does hemoglobin have a higher affinity for CO than O2

Hemoglobin has a higher affinity for CO because it is smaller and it forms bonds at a straight angle. Triple bound C to O has a smaller distance than double bound O to O

14

Sickle cell anemia is caused by what mutation?

Glu --> Val at 6th position, in beta globin chain of hemoglobin, which changes from a polar to nonpolar amino acid

15

What are the ramifications of sickle cell anemia mutation

Mutation causes RBC to change its shape, which decreases O2 carrying capacity and elasticity.