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- W2092809012 endingPage "1159" @default.
- W2092809012 startingPage "1129" @default.
- W2092809012 abstract "I. Introduction II. Classification of Plant Prxs and Their Distribution in Plants and Cyanobacteria III. Peroxidase Activity of Peroxiredoxins IV. Conformational Dynamics and Interacting Partners of Prx In Vitro and In Vivo V. Typical 2-Cys Peroxiredoxins A. Characteristics of 2-CysPrxs B. Reduction of oxidized 2-CysPrx C. Consequences of 2-CysPrx deficiency VI. Peroxiredoxin Q, an Atypical 2-CysPrx of Chloroplasts and Cyanobacteria VII. 1-Cysteine Peroxiredoxin VIII. Type II Peroxiredoxins, the Most Widely Distributed Atypical 2-CysPrxs in Plants A. Principle features of type II Prx B. Cytosolic PrxII C. Plastid PrxIIE D. Mitochondrial PrxIIF E. Cyanobacterial type II Prx IX. Plant Glutathione Peroxidases X. Posttranslational Regulation of Peroxiredoxin Activities A. Hyperoxidation and sulfiredoxin B. Nitrosylation C. Other posttranslational Prx modifications XI. Role of Peroxiredoxins in Plant Metabolism A. Plastids and photosynthesis B. Mitochondria and respiration XII. Peroxiredoxins as Chaperone and in Plant Redox Signaling A. Prx as chaperone B. Prx in ROS-dependent signaling C. Prx in RNS-dependent signaling XIII. Regulation of Peroxiredoxin Gene Expression A. Basal pattern of Prx expression and developmental control B. Regulation of plastid Prx expression by retrograde signaling C. Stress-dependent regulation XIV. Additional Functions of Peroxiredoxins in Plants XV. Outlook Peroxiredoxins (Prx) are central elements of the antioxidant defense system and the dithiol-disulfide redox regulatory network of the plant and cyanobacterial cell. They employ a thiol-based catalytic mechanism to reduce H2O2, alkylhydroperoxide, and peroxinitrite. In plants and cyanobacteria, there exist 2-CysPrx, 1-CysPrx, PrxQ, and type II Prx. Higher plants typically contain at least one plastid 2-CysPrx, one nucleo-cytoplasmic 1-CysPrx, one chloroplast PrxQ, and one each of cytosolic, mitochondrial, and plastidic type II Prx. Cyanobacteria express variable sets of three or more Prxs. The catalytic cycle consists of three steps: (i) peroxidative reduction, (ii) resolving step, and (iii) regeneration using diverse electron donors such as thioredoxins, glutaredoxins, cyclophilins, glutathione, and ascorbic acid. Prx proteins undergo major conformational changes in dependence of their redox state. Thus, they not only modulate cellular reactive oxygen species- and reactive nitrogen species-dependent signaling, but depending on the Prx type they sense the redox state, transmit redox information to binding partners, and function as chaperone. They serve in context of photosynthesis and respiration, but also in metabolism and development of all tissues, for example, in nodules as well as during seed and fruit development. The article surveys the current literature and attempts a mostly comprehensive coverage of present day knowledge and concepts on Prx mechanism, regulation, and function and thus on the whole Prx systems in plants. Antioxid. Redox Signal. 15, 1129–1159." @default.
- W2092809012 created "2016-06-24" @default.
- W2092809012 creator A5012666877 @default.
- W2092809012 date "2011-08-15" @default.
- W2092809012 modified "2023-10-16" @default.
- W2092809012 title "Peroxiredoxins in Plants and Cyanobacteria" @default.
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