Wavelength dependence of the geometric and structural photoisomerization of bilirubin bound to human serum albumin.
The two quantitatively important photoisomers in bilirubin metabolism during phototherapy are (ZE)-bilirubin and (EZ)-cyclobilirubin. We describe in vitro studies on the wavelength dependence for the geometric (delta 4Z, delta 15Z----delta 4Z, delta 15E) and structural (endovinyl cyclization) photoisomerization of bilirubin bound to human serum albumin by a high performance liquid chromatography method. For the geometric photoisomerization from (ZZ)-bilirubin to (ZE)-bilirubin, the most effective wavelength in vitro was 410 nm. For the structural photoisomerization, green light at 510 nm is the most efficient for causing cyclization of (ZZ)-bilirubin to (EZ)-cyclobilirubin via (EZ)-bilirubin and this may depend on a larger cross-section of (EZ)-bilirubin than (ZZ)-bilirubin in this spectral region and/or on a larger quantum yield for cyclization than geometric photoisomerization.
D001663:Bilirubin / Q000031:analogs & derivatives / Q000097:blood / Q000528:radiation effects*; D002851:Chromatography, High Pressure Liquid; D003500:Cyclization; D006801:Humans; D066298:In Vitro Techniques; D007536:Isomerism; D010777:Photochemistry; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism
D012709:Serum Albumin; C041079:cyclobilirubin; D001663:Bilirubin