Structural Biological Study of Biliverdin Reductase.
Akihiro Kikuchi
Abstract
Open-access reader
Akihiro Kikuchi
Abstract
Open-access reader
In mammals, heme is degraded to biliverdin by heme oxygenase (HO) and subsequently, the biliverdin is reduced to bilirubin by biliverdin reductase (BVR) . The metabolic waste product, bilirubin is now becoming recognized as having functional importance. It appears to play a key role in oxidative stress defense in vivo. Thus, heme degradation pathway has seen renewed interest in its biosynthesis. Recently, the X-ray crystal structures of HO and BVR were determined. Based on the structures, new insights into the mechanism of the heme degradation and bilirubin synthesis are discussed.
A significance statement is not available in the OpenAlex record.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
In mammals, heme is degraded to biliverdin by heme oxygenase (HO) and subsequently, the biliverdin is reduced to bilirubin by biliverdin reductase (BVR) . The metabolic waste product, bilirubin is now becoming recognized as having functional importance. It appears to play a key role in oxidative stress defense in vivo. Thus, heme degradation pathway has seen renewed interest in its biosynthesis. Recently, the X-ray crystal structures of HO and BVR were determined. Based on the structures, new insights into the mechanism of the heme degradation and bilirubin synthesis are discussed.
Key concepts: Biliverdin reductase, Biliverdin, Bilirubin, Heme, Heme oxygenase, Biochemistry, Chemistry, Reductase