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Biochemistry-Test 2 Lecture 32-33

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Master the complexities of human physiology with this comprehensive textbook, covering topics such as blood transport, gas exchange, and oxygen binding. Dive deeper into the world of hemoglobin, myoglobin, and denatured hemoglobin, and explore the intricate mechanisms that regulate oxygen binding and release.

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Biochemistry

Test 2 Lecture 32-33




Compiled By Simon Mwangi
Edition: 2024/25

, Science | Biochemistry I of XIII pages
1. ___ is the O2 carrier protein of the blood.
hemoglobin

2. ___ is an O2 storage protein found in muscle
myoglobin

3. Hemoglobin has a _______ affinity for O2 in the lungs, which promotes O2 uptake and has a ____ affinity
high
lower
protein intelligence

4. Hemoglobin assists in the transport of CO2 from ___ to the ___
tissues
lung

5. High concentrations of ___ provide an O2 reserve in the muscles of diving birds and mammals.
myoglobin
store O2 in muscles, dont need to breathe when diving

6. Myoglobin is composed of ___ helixes
aplha

7. The heme of myoglobin is bound ___
tightly but not covalently, can come off under extreme conditions

8. Heme is attached to myoglobin by ___ and ___
proximal histidine
distal histidine

9. The proximal histidine of myoglobin attaches to the ___
the distal histidine ___
iron of the heme
hovers above where O2 will bind, Water sits in that places when waiting for O2

10. iron in hemoglobin is in the ___ state
+2

11. when O2 is not bound to iron of hemoglobin the iron is ___
when O2 is bound to the iron of hemoglobin the iron is ___
big and pulled down by the proximal histidine
now in +3 state, gets smaller and is pulled in line with the heme




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