Toward a Mechanism for Biliprotein Lyases: Revisiting Nucleophilic Addition to Phycocyanobilin

被引:13
作者
Tu, Jun-Ming [1 ,2 ,3 ]
Zhou, Ming [2 ,3 ]
Haessner, Rainer [4 ]
Ploescher, Matthias [1 ]
Eichacker, Lutz [1 ]
Scheer, Hugo [1 ]
Zhao, Kai-Hong [2 ,3 ]
机构
[1] Univ Munich, Dept Biol Bot 1, D-80638 Munich, Germany
[2] Huazhong Agr Univ, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China
[3] Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Wuhan 430074, Peoples R China
[4] Tech Univ Munich, Inst Organ Chem, D-85748 Garching, Germany
基金
中国国家自然科学基金;
关键词
CHROMOPHORE ATTACHMENT; PYRROLE PIGMENTS; BILE-PIGMENTS; PROTEIN; PHYCOERYTHROCYANIN; PHYCOBILIPROTEINS; SPECIFICITY; SUBUNIT; MODEL; PHOTOCHEMISTRY;
D O I
10.1021/ja9002348
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Biliprotein lyases attach linear-tetrapyrrolic bilins covalently to apoproteins, which is a prerequisite for the assembly of phycobiliproteins into phycobilisomes, the light-harvesting complexes of cyanobacteria. On the basis of the addition of thiol and imidazole to phycocyanobilin, we propose a generalized lyase reaction mechanism. The adducts contain isomerized phycocyanobilin that can be transferred by the lyase to apoproteins by either back-isomerization, generating phycocyanobilin-containing proteins, or direct transfer, generating phycoviolobilin-containing proteins.
引用
收藏
页码:5399 / +
页数:4
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