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motee motee
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6 years ago
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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KeezeKeeze
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6 years ago
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motee Author
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this is exactly what I needed
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Helped a lot
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