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Which consequence results when the *crystal field splitting* is disrupted in myoglobin?

A)Reduced oxygen binding affinity occurs
B)Hydrophobic collapse within the dimer occurs
C)Significant disulfide bridge formation occurs
D)Increased protein glycosylation subsequently occurs

💡 Explanation

Reduced oxygen affinity occurs because disruption directly impacts *crystal field splitting*, a mechanism essential for iron's electronic configuration and subsequent proper O2 binding, therefore affinity lessens rather than being enhanced or affecting glycosylation or hydrophobic interactions.

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