Cyanobacterial Oxygenic Photosynthesis is Protected by Flavodiiron Proteins

Life

Yagut Allahverdiyeva²  Janne Isojärvi²  Pengpeng Zhang¹  Eva-Mari Aro¹  John C. Meeks² 

[1] Molecular Plant Biology, Department of Biochemistry, University of Turku, FI-20014 Turku, Finland;

关键词: flavodiiron protein;    flavoprotein;    cyanobacteria;    Mehler-like reaction;    nitrogenase;    photosystem;    photodamage;    electron transfer;    photosynthesis;    phycobilisome;    photoprotection;   

DOI  :  10.3390/life5010716

来源: mdpi

【 摘 要 】

Flavodiiron proteins (FDPs, also called flavoproteins, Flvs) are modular enzymes widely present in Bacteria and Archaea. The evolution of cyanobacteria and oxygenic photosynthesis occurred in concert with the modulation of typical bacterial FDPs. Present cyanobacterial FDPs are composed of three domains, the β-lactamase-like, flavodoxin-like and flavin-reductase like domains. Cyanobacterial FDPs function as hetero- and homodimers and are involved in the regulation of photosynthetic electron transport. Whilst Flv2 and Flv4 proteins are limited to specific cyanobacterial species (β-cyanobacteria) and function in photoprotection of Photosystem II, Flv1 and Flv3 proteins, functioning in the “Mehler-like” reaction and safeguarding Photosystem I under fluctuating light conditions, occur in nearly all cyanobacteria and additionally in green algae, mosses and lycophytes. Filamentous cyanobacteria have additional FDPs in heterocyst cells, ensuring a microaerobic environment for the function of the nitrogenase enzyme under the light. Here, the evolution, occurrence and functional mechanisms of various FDPs in oxygenic photosynthetic organisms are discussed.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.