Near-infrared spectra of Scapharca homodimeric hemoglobin: characterization of the deoxy and photodissociated derivatives.
The near-infrared charge transfer band at 760 nm (band III) has been investigated in deoxy and photodissociated dimeric Scapharca hemoglobin. At 300 K, the 10-ns spectrum of the carbonmonoxy derivative photoproduct is shifted by about 6 nm toward longer wavelengths with respect to the deoxy spectrum, both in buffer and in glycerol/buffer solutions. Moreover, the band III peak occurs at about the same wavelength at 300 K and at 10 K for the 10-ns photodissociated derivative, whereas in the deoxy derivative large changes in peak position and linewidth are observed as a function of temperature. These findings suggest that in dimeric Scapharca hemoglobin the photoproduct has not relaxed after 10 ns. The complete time dependence of the relaxation process has been studied both in buffer and in glycerol/buffer solutions at room temperature. The relaxation from the photoproduct to the deoxy species occurs on a microsecond time scale, in line with recent optical absorption and resonance Raman measurements.
Huang
J
J
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Leone
M
M
Boffi
A
A
Friedman
J M
JM
Chiancone
E
E
D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D049872:Bivalvia; D002263:Carboxyhemoglobin / Q000737:chemistry; D019281:Dimerization; D006441:Hemoglobin A / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry* / Q000528:radiation effects; D006455:Hemoglobins, Abnormal / Q000737:chemistry; D010777:Photochemistry; D011487:Protein Conformation; D019265:Spectroscopy, Near-Infrared; D013696:Temperature
D006454:Hemoglobins; D006455:Hemoglobins, Abnormal; C083082:dimeric hemoglobin, Scapharca inaequivalvis; C100003:deoxyhemoglobin; D006441:Hemoglobin A; C026236:hemoglobin I, non-mammalian; D002263:Carboxyhemoglobin