Why Does Myoglobin Have a Histidine That Prevents Both O₂

question 10

Multiple Choice

Why does myoglobin have a histidine that prevents both O₂ and CO from binding perpendicularly to the heme plane?

• A) This increases myoglobin's affinity for O₂.
• B) This increases myoglobin's affinity for CO.
• C) This lessens the difference in myoglobin's affinity for CO versus O₂.
• D) This prevents the iron of the heme from being oxidized.

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