The malaria-causing parasite Plasmodium falciparum is a severe threat to human health across the globe. This parasite alone causes the highest morbidity and mortality than any other species of Plasmodium. The parasites dynamically multiply in the erythrocytes of the vertebrate hosts, a large number of reactive oxygen species that damage biological macromolecules are produced in the cell during parasite growth. To relieve this intense oxidative stress, the parasite employs an NADPH-dependent thioredoxin and glutathione system that acts as an antioxidant and maintains redox status in the parasite. The mutual interaction of both redox proteins is involved in various biological functions and the survival of the erythrocytic stage of the parasite. Since the Plasmodium species is deficient in catalase and classical glutathione peroxidase, so their redox balance relies on a complex set of five peroxiredoxins, differentially positioned in the cytosol, mitochondria, apicoplast, and nucleus with partly overlapping substrate preferences. Moreover, Plasmodium falciparum possesses a set of members belonging to the thioredoxin superfamily, such as three thioredoxins, two thioredoxin-like proteins, one dithiol, three monocysteine glutaredoxins, and one redox-active plasmoredoxin with largely redundant functions. This review paper aims to discuss and encapsulate the biological function and current knowledge of the functional redox network of Plasmodium falciparum.

导致疟疾的寄生虫恶性疟原虫对全球人类健康构成严重威胁。这种寄生虫比其他疟原虫引起最高的发病率和死亡率。寄生虫在脊椎动物宿主的红细胞中动态繁殖，在寄生虫生长期间，细胞中会产生大量破坏生物大分子的活性氧。为了缓解这种强烈的氧化应激，该寄生虫采用了NADPH依赖性的硫氧还蛋白和谷胱甘肽系统，该系统可作为抗氧化剂并维持该寄生虫的氧化还原状态。两种氧化还原蛋白的相互作用都参与了各种生物学功能以及该寄生虫的红细胞阶段的存活。自疟原虫的物种缺乏过氧化氢酶和经典的谷胱甘肽过氧化物酶，因此它们的氧化还原平衡依赖于五种过氧化物酶的复杂集合，它们在细胞质，线粒体，apicoplast和细胞核中的位置不同，底物偏好部分重叠。此外，恶性疟原虫具有一组属于硫氧还蛋白超家族的成员，例如三种硫氧还蛋白，两种硫氧还蛋白样蛋白，一种二硫醇，三种单半胱氨酸戊二醛毒素和一种具有很大程度上冗余功能的氧化还原活性血浆绒毛毒素。本文旨在讨论和封装恶性疟原虫功能氧化还原网络的生物学功能和最新知识。