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Nat Commun ; 8: 14397, 2017 02 07.
Article in English | MEDLINE | ID: mdl-28169272

ABSTRACT

Biliverdin reductase catalyses the last step in haem degradation and produces the major lipophilic antioxidant bilirubin via reduction of biliverdin, using NAD(P)H as a cofactor. Despite the importance of biliverdin reductase in maintaining the redox balance, the molecular details of the reaction it catalyses remain unknown. Here we present the crystal structure of biliverdin reductase in complex with biliverdin and NADP+. Unexpectedly, two biliverdin molecules, which we designated the proximal and distal biliverdins, bind with stacked geometry in the active site. The nicotinamide ring of the NADP+ is located close to the reaction site on the proximal biliverdin, supporting that the hydride directly attacks this position of the proximal biliverdin. The results of mutagenesis studies suggest that a conserved Arg185 is essential for the catalysis. The distal biliverdin probably acts as a conduit to deliver the proton from Arg185 to the proximal biliverdin, thus yielding bilirubin.


Subject(s)
Biliverdine/chemistry , Cyanobacteria/metabolism , NADP/chemistry , Oxidoreductases Acting on CH-CH Group Donors/metabolism , Arginine/chemistry , Bilirubin/metabolism , Biliverdine/metabolism , Binding Sites , Biocatalysis , Coenzymes/chemistry , Coenzymes/metabolism , Crystallography, X-Ray , Models, Molecular , Mutagenesis , NADP/metabolism , Oxidoreductases Acting on CH-CH Group Donors/chemistry , Oxidoreductases Acting on CH-CH Group Donors/genetics , Protein Binding , Protein Structure, Tertiary , Structure-Activity Relationship , Substrate Specificity
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