Photo-dissociation quantum yields of mammalian oxyhemoglobin investigated by a nanosecond laser technique

• Published in: Biochemical and biophysical research communications Vol. 353; no. 4; pp. 953 - 959
• Main Authors: Yang, Ning-li, Zhang, Shu-yi, Kuo, Pao-kuang, Qu, Min, Fang, Jian-wen, Li, Jia-huang, Hua, Zi-chun
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 23.02.2007
• Subjects: 60 APPLIED LIFE SCIENCES; AMINO ACID SEQUENCE; Animals; CATTLE; HEMOGLOBIN; HORSES; Humans; Hydrophobic and Hydrophilic Interactions; Kinetics; Lasers; Light; Models, Molecular; Molecular Sequence Data; Nanotechnology - methods; Oxyhemoglobin; Oxyhemoglobins - chemistry; PH VALUE; Photo-dissociation; Photochemistry - methods; Protein Conformation; Quantum Theory; Quantum yield; RABBITS; Sequence Homology, Amino Acid; Species Specificity; Spectrophotometry - instrumentation; Spectrophotometry - methods; SWINE; Time Factors; Quantum yield; Photo-dissociation; Oxyhemoglobin
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/j.bbrc.2006.12.118

The photo-dissociations of oxyhemoglobin of several mammals, such as human, bovine, pig, horse, and rabbit, have been studied. By means of optical pump-probe technique, the quantum yields for photo-dissociation of these oxyhemoglobin have been determined at pH 7 and 20 °C. A nanosecond laser at 532 nm is used as the pumping source, and a xenon lamp through a monochrometer provides a probe light at 432 nm. The experimental results show that the quantum yields of these mammalian oxyhemoglobin are different from each other, especially for that of rabbit. By analyzing the amino acid sequences and tetramer structures as well as the flexibility and hydrophobicity of the different hemoglobin, possible explanations for the differences are proposed.