The photoproduct of carbon monoxide myoglobin generated at 4 K and lower has a resonance Raman spectrum characteristic of a high-spin heme but in which the high-frequency core size-sensitive lines are at lower frequency than those in the deoxy preparation. Such differences are not detected in the photoproduct generated at higher temperatures (50 K) or in that generated at room temperature with 10-nsec pulses. The data indicate that at the low temperature (4 K), the heme in the photoproduct is not fully relaxed, and from the data we conclude that the photoproduct has an expanded porphyrin core. We infer that the core size exceeds that in deoxymyoglobin because the rigid protein prevents the high-spin iron atom from moving to its full out-of-plane displacement at the very low temperatures.
|Original language||English (US)|
|Number of pages||5|
|Journal||Proceedings of the National Academy of Sciences of the United States of America|
|State||Published - 1986|
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