Kikuchi A, Park S Y, Miyatake H, Sun D, Sato M, Yoshida T, Shiro Y
RIKEN Harima Institute/SPring-8, Sayo, Hyogo 679-5148, Japan.
Nat Struct Biol. 2001 Mar;8(3):221-5. doi: 10.1038/84955.
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.
胆绿素还原酶（BVR）是一种可溶性细胞质酶，它以NADH或NADPH作为电子供体，催化胆绿素转化为胆红素。胆红素是一种重要的生物抗氧化剂，但它也具有神经毒性，是核黄疸的病因。在本研究中，我们测定了大鼠BVR在1.4埃分辨率下的晶体结构。该结构包含两个结构域：一个具有二核苷酸结合折叠（罗斯曼折叠）特征的N端结构域和一个主要由反平行六链β-折叠组成的C端结构域。基于此结构，我们提出了NAD(P)H和胆绿素的结合模式以及该酶的一种可能机制。
