Multiple Choice
The distal histidine residue in myoglobin acts to:
8. Protein Function
Heme Prosthetic Group
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In hemoglobin, the equilibrium transition from T state to R state is triggered by:
A
Fe2+ binding.
B
Heme binding.
C
Oxygen binding.
D
Protease cleavage.
Verified step by step guidance1
Understand the structure of hemoglobin: Hemoglobin is a protein composed of four subunits, each containing a heme group capable of binding oxygen.
Identify the T and R states: The T (tense) state is the low-affinity state for oxygen, while the R (relaxed) state is the high-affinity state.
Recognize the role of oxygen: Oxygen binding to the heme group in one of the subunits induces a conformational change in hemoglobin.
Explain the transition: The binding of oxygen to the heme group causes a shift from the T state to the R state, increasing the affinity for oxygen in the remaining subunits.
Conclude the mechanism: This cooperative binding mechanism is essential for efficient oxygen transport and release in tissues.
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