Hemoglobin and Myoglobin Flashcards
Hemeprotein
proteins with heme as tightly bound prosthetic group
Prosthetic Group
coenzyme permanently associated with enzyme or protein
Cytochromes
heme group serves as electron carrier that can be oxidized and reduced
in ETC
Catalase
heme is part of active site of enzyme that catalyzes breakdown of hydrogen peroxide
in peroxisomes
Heme use in Myoglobin and Hemoglobin
heme used to reversibly bind oxygen
Heme Structure
iron in center of porphyrin ring
makes 6 bonds- 4 to iron, 1 to R group of histidine of globin, 1 to oxygen
Myoglobin
in heart and skeletal m
O reservoir; carrier that increases transport rate w/in muscle cells
Hemoglobin
Red Blood Cells
transports 4 O2 mol from lungs to capillaries of tissues
transports CO2 and H from tissues to lungs
T Form
deoxy form when no O bound
low O affinity
R Form
O binding causes break of some polar bonds of T form
high O affinity
O binding myoglobin vs hemoglobin
1 O to Myoglobin
4 O to Hemoglobin
Myoglobin has higher affinity
Bohr Effect
Decreases O affinity at lower pH
shifts curve to right
stabilizes T form
2,3 BPG
stabilizes T form
decreases O affinity
shifts curve right
CO2 Binding
stabilizes T form
less O affinity
shifts curve right
CO Binding
hemoglobin has higher affinity for CO than O; binds more closely
higher O affinity
R form
Shifts curve left