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  • Title: Crystal structure of rat biliverdin reductase.
    Author: Kikuchi A, Park SY, Miyatake H, Sun D, Sato M, Yoshida T, Shiro Y.
    Journal: Nat Struct Biol; 2001 Mar; 8(3):221-5. PubMed ID: 11224565.
    Abstract:
    Biliverdin reductase (BVR) is a soluble cytoplasmic enzyme that catalyzes the conversion of biliverdin to bilirubin using NADH or NADPH as electron donor. Bilirubin is a significant biological antioxidant, but it is also neurotoxic and the cause of kernicterus. In this study, we have determined the crystal structure of rat BVR at 1.4 A resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that is predominantly an antiparallel six-stranded beta-sheet. Based on this structure, we propose modes of binding for NAD(P)H and biliverdin, and a possible mechanism for the enzyme.
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