Biliverdin reduction by cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates.
Biliverdin reduction by cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates.
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蓝藻藻蓝蛋白：铁氧还蛋白氧化还原酶（PcyA）通过线性四吡咯自由基中间体进行胆绿素还原。
DOI：
10.1021/ja049280z
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发表时间：
2004
影响因子：
15
通讯作者：
Lagarias,JClark
中科院分区：
文献类型：
--
作者：
Tu,Shih-Long;Gunn,Alexander;Toney,MichaelD;Britt,RDavid;Lagarias,JClark
蓝藻绿胆素：铁氧化还蛋白氧化还原酶（PcyA）催化胆绿素IXα (BV)的四电子还原生成藻蓝胆素，这是蓝藻光敏色素线性四吡啶（bilin）假基和捕光藻胆蛋白生物合成的关键步骤。使用厌氧分析方案，在PcyA催化循环中产生的光学检测到的十亿蛋白中间体被证明与在低温下测量的各向各向≈2 EPR信号的外观和衰减密切相关。胆绿素XIIIα还原的吸收光谱模拟支持从铁氧还蛋白到质子化的胆红素：PcyA复合物的直接电子转移机制。
Cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes the four electron reduction of biliverdin IXα (BV) to phycocyanobilin, a key step in the biosynthesis of the linear tetrapyrrole (bilin) prosthetic groups of cyanobacterial phytochromes and the light-harvesting phycobiliproteins. Using an anaerobic assay protocol, optically detected bilin-protein intermediates, produced during the PcyA catalytic cycle, were shown to correlate well with the appearance and decay of an isotropicg≈ 2 EPR signal measured at low temperature. Absorption spectral simulations of biliverdin XIIIα reduction support a mechanism involving direct electron transfers from ferredoxin to protonated bilin:PcyA complexes.