Time-resolved resonance raman spectroscopy of hemoglobin derivatives: heme structure changes in 7 nanoseconds.
Resonance Raman spectra of oxyhemoglobin, deoxyhemoglobin, carboxyhemoglobin, and the corresponding myoglobin derivatives have been obtained with 7-nanosecond laser pulses at 531.8 nanometers. The results suggest that no transient constraint of the heme group by the globin structure occurs on this time scale, and thus establish a temporal sequence for the early events that may participate in the stereochemical trigger mechanism of hemoglobin cooperativity.
D000494:Allosteric Regulation; D002263:Carboxyhemoglobin; D006418:Heme; D006454:Hemoglobins; D007700:Kinetics; D009211:Myoglobin; D010108:Oxyhemoglobins; D013059:Spectrum Analysis, Raman
D006454:Hemoglobins; D009211:Myoglobin; D010108:Oxyhemoglobins; D006418:Heme; D002263:Carboxyhemoglobin