Ultrafast catalytic processes and conformational changes in the light-driven enzyme protochlorophyllide oxidoreductase (POR).
Ultrafast catalytic processes and conformational changes in the light-driven enzyme protochlorophyllide oxidoreductase (POR).
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DOI：
10.1042/bst0370387
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发表时间：
2009-04
影响因子：
3.9
通讯作者：
O. Sytina;D. Heyes;C. N. Hunter;Marie Louise Groot-Marie Louise-Groot-2252530298
中科院分区：
文献类型：
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作者：
O. Sytina;D. Heyes;C. N. Hunter;Marie Louise Groot-Marie Louise-Groot-2252530298
POR（原叶绿素内酯氧化还原酶）属于乙醇脱氢酶家族，在吸收光时将原叶绿素内酯还原为脱氧绿叶素。该还原涉及两个质子和两个电子的转移，是叶绿素生物合成中的重要调节步骤。近年来，由于大量纯酶的可用性，许多催化反应已经通过使用各种光谱方法（包括催化中的超快初始事件）被阐明。此外，已经证明蛋白质的光激活构象变化对于激活催化作用是必要的。这使得POR成为研究酶的结构变化和功能之间关系的非常重要的模型系统。
The enzyme POR (protochlorophyllide oxidoreductase), from the family of alcohol dehydrogenases, reduces protochlorophyllide into chlorophyllide on the absorption of light. The reduction involves the transfer of two protons and two electrons and is an important regulatory step in the biosynthesis of chlorophyll. In recent years, due to the availability of large quantities of the pure enzyme, much of the catalytic reaction has been unravelled by using a variety of spectroscopic methods, including ultrafast initial events in catalysis. In addition, it has been demonstrated that a light-activated conformational change of the protein is necessary to activate catalysis. This makes POR a very important model system to study the relationship between structural changes of enzymes and functionality.