Enzymatic Activity and Thermodynamic Stability of Biliverdin IXβ Reductase Are Maintained by an Active Site Serine-Reference-Cited by-同舟云学术

Enzymatic Activity and Thermodynamic Stability of Biliverdin IXβ Reductase Are Maintained by an Active Site Serine

Published:2017-01-11 Issue:8 Volume:23 Page:1891-1900
ISSN:0947-6539
Container-title:Chemistry - A European Journal
language:en
Short-container-title:Chem. Eur. J.

Author:

Chu Wen-Ting¹,Nesbitt Natasha M.²,Gnatenko Dmitri V.²,Li Zongdong²,Zhang Beibei³,Seeliger Markus A.⁴,Browne Seamus⁵,Mantle Timothy J.⁵,Bahou Wadie F.²,Wang Jin¹⁶

Affiliation:

1. State Key Laboratory of Electroanalytical Chemistry; Changchun Institute of Applied Chemistry; Chinese Academy of Sciences, Changchun; Jilin 130022 P. R. China

2. Department of Medicine; Stony Brook University; Stony Brook NY 11794 USA

3. Department of Biochemistry and Cell Biology; Stony Brook University; Stony Brook NY 11794 USA

4. Department of Pharmacological Sciences; Stony Brook University; Stony Brook NY 11794 USA

5. Department of Biochemistry; Trinity College; Dublin 2 Ireland

6. Department of Chemistry and Physics; Stony Brook University; Stony Brook NY 11794 USA

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Reference70 articles.

1. Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme

2. Changes in the Composition of Bilirubin-IX Isomers During Human Prenatal Development

3. Computational and experimental studies on the catalytic mechanism of biliverdin-IXβ reductase

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