Abstract
The substrate specificity of rat liver biliverdin reductase was probed using helical and extended biliverdins. The former were the ZZZ-all-syn biliverdins IX α and IX γ, and the latter were the 5Z-syn, 10Z-syn, 15z-anti; 5Z-anti, 10Z-syn, 15Z-anti; 5Z-syn, 10E-anti, 15Z-syn; 5Z-syn, 10E-anti, 15Z-anti and 5Z-anti, 10E-anti, 15E-anti biliverdins. It was found that the reduction rates of the biliverdins increased with the progressive stretching of their conformations. The most extended biliverdin was reduced at a higher rate than biliverdin IX α. The chemical reduction rates to bilirubins followed a similar pattern. Nuceophilic ad dition of 2-mercaptoethanol to the C10 methine was also favored in the extended biliverdins.
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