Crystal structure of rat biliverdin reductase

@article{Kikuchi2001CrystalSO,
  title={Crystal structure of rat biliverdin reductase},
  author={Akihiro Kikuchi and Sam-Yong Park and Hideyuki Miyatake and Danyu Sun and Michihiko Sato and Tadashi Yoshida and Yoshitsugu Shiro},
  journal={Nature Structural Biology},
  year={2001},
  volume={8},
  pages={221-225}
}
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 Å resolution. The structure contains two domains: an N-terminal domain characteristic of a dinucleotide binding fold (Rossmann fold) and a C-terminal domain that… 
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Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex.
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity
TLDR
Unexpectedly, two biliverdin molecules, which are designated the proximal and distal biliverdins, bind with stacked geometry in the active site and support that a conserved Arg185 is essential for the catalysis.
Enzymatic Activity and Thermodynamic Stability of Biliverdin IXβ Reductase Are Maintained by an Active Site Serine.
TLDR
Experimental and thermodynamic modeling studies are undertaken to provide further insight into the role of the cofactor in substrate accessibility and protein folding properties regulating BLVRB catalytic mechanisms and defines a dynamic model for apoBLVRB extending beyond the crystal structure of the binary BLVRb/NADP+ complex.
Bilin-metabolizing enzymes: site-specific reductions catalyzed by two different type of enzymes.
Activation of biliverdin-IXalpha reductase by inorganic phosphate and related anions.
TLDR
Evidence is presented that the apparent peak of activity observed at neutral pH with phosphate buffer and NADH as cofactor is an anion-dependent activation, where inorganic phosphate apparently mimics the role played by the 2'-phosphate of NADPH in stabilizing the interaction between NADH and the enzyme.
Expression, purification and preliminary X-ray crystallographic analysis of cyanobacterial biliverdin reductase.
  • A. Watanabe, K. Hirata, K. Wada
  • Chemistry
    Acta crystallographica. Section F, Structural biology and crystallization communications
  • 2011
TLDR
The structure of cyanobacterial BVR may provide insights into the mechanisms of its enzymatic and physiological functions.
On how the conformation of biliverdins influences their reduction to bilirubins: a biological and molecular modeling study.
New insights into biliverdin reductase functions: linking heme metabolism to cell signaling.
TLDR
These, together with the protein's primary and secondary features, intimately link BVR to the entire spectrum of cell-signaling cascades.
Biliverdin Reductase: More than a Namesake – The Reductase, Its Peptide Fragments, and Biliverdin Regulate Activity of the Three Classes of Protein Kinase C
TLDR
Small fragments of hBVR are potent activators and inhibitors of the ERK kinases and PKCs: as such, they suggest the potential application of BVR-based technology in therapeutic settings.
Biliverdin reductase in cardiovascular inflammation
TLDR
It is shown that BVR acts in an anti-inflammatory manner in the endothelium; by increasing eNOS activation and nitric oxide release, inducing HO-1 protein expression and by inhibiting TNFα-induced leukocyte-endothelium interaction.
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References

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TLDR
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