氧化还原酶
生物化学
跨膜结构域
化学
抗坏血酸
跨膜蛋白
蛋白质结构
氨基酸
生物
酶
立体化学
生物物理学
食品科学
受体
作者
Peilong Lu,Dan Ma,Chuangye Yan,Xinqi Gong,Mingjian Du,Yigong Shi
标识
DOI:10.1073/pnas.1323931111
摘要
Significance Vitamin C (also known as ascorbate), an essential nutrient for humans, plays an important role in protection against oxidative stress. The ascorbate-dependent oxidoreductase cytochrome b 561 (Cyt b 561 ) is a family of highly conserved, multipass transmembrane enzymes found only in eukaryotes. Cyt b 561 plays a key role in ascorbate recycling and many other important physiological processes, such as iron absorption. The atomic structure and functional mechanism of Cyt b 561 remain unknown. In this study, we report the high-resolution crystal structures of Cyt b 561 in both ascorbate-free and ascorbate-bound states. Our structural and biochemical analyses identify a general functional mechanism for the Cyt b 561 family.
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