期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 59, 期 -, 页码 73-80出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2019.03.005
关键词
-
资金
- Japan Society for the Promotion of Science (JSPS) KAKENHI from MEXT [16K07280, 20770092, 25840026, 16H04754, 22770096, 24570122, 16K07261, 23370052]
- Japan Science and Technology Agency (JST)-Mirai Program
- Takeda Science Foundation, JAPAN
- Ibaraki Prefecture's Sendokenkyu
- Platform Project for Supporting Drug Discovery and Life Science Research (BINDS) from Japan Agency for Medical Research and Development (AMED) [JP18am0101001]
- Grants-in-Aid for Scientific Research [22770096, 16H04754, 20770092, 16K07280, 23370052, 24570122, 16K07261, 25840026] Funding Source: KAKEN
In mammals, the green heme metabolite biliverdin is converted to a yellow anti-oxidant by NAD(P)H-dependent biliverdin reductase (BVR), whereas in O-2-dependent photosynthetic organisms it is converted to photosynthetic or light-sensing pigments by ferredoxin-dependent bilin reductases (FDBRs). In NADP(+)-bound and biliverdin-bound BVR-A, two biliverdins are stacked at the binding cleft; one is positioned to accept hydride from NADPH, and the other appears to donate a proton to the first biliverdin through a neighboring arginine residue. During the FDBR-catalyzed reaction, electrons and protons are supplied to bilins from ferredoxin and from FDBRs and waters bound within FDBRs, respectively. Thus, the protonation sites of bilin and catalytic residues are important for the analysis of site-specific reduction. The neutron structure of FDBR sheds light on this issue.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据