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. 2001 Mar;8(3):221-5.
doi: 10.1038/84955.

Crystal structure of rat biliverdin reductase

A Kikuchi  1 , S Y Park, H Miyatake, D Sun, M Sato, T Yoshida, Y Shiro
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Crystal structure of rat biliverdin reductase

A Kikuchi et al. Nat Struct Biol. 2001 Mar.

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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  • Turning green to gold.
    McDonagh AF. McDonagh AF. Nat Struct Biol. 2001 Mar;8(3):198-200. doi: 10.1038/84915. Nat Struct Biol. 2001. PMID: 11224558 No abstract available.

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