Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 572, Issue -, Pages 151-156Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2021.07.091
Keywords
Pyruvate synthase; Oxidoreductase; Ferredoxin; CO2-fixing enzyme; Anaerobic
Categories
Funding
- Strategic Priority Research Program of the Chinese Academy of Sciences [XDPB18]
- National Science Foundation of China [31870038]
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This study investigated the reductive carboxylation activities of six heterotetrameric PFORs from hyperthermophilic archaea, revealing diversity in their functions. Among them, PFORpfm from Pyrolobus fumarii showed the highest reductive carboxylation activities and red/ox ratio, indicating the potential significance of PFOR in autotrophic CO2 fixation in high temperature environments.
Pyruvate synthase (pyruvate:ferredoxin oxidoreductase, PFOR) catalyzes the interconversion of acetylCoA and pyruvate, but the reductive carboxylation activities of heterotetrameric PFORs remain largely unknown. In this study, we cloned, expressed, and purified selected six heterotetrameric PFORs from hyperthermophilic archaea. The reductive carboxylation activities of these heterotetrameric PFORs were measured at 70 degrees C and the ratio of reductive carboxylation activity to oxidative decarboxylation activity (red/ox ratio) were calculated. Four out of six showed reductive decarboxylation activities. Among them, the PFORpfm from Pyrolobus fumarii showed the highest reductive carboxylation activities and the highest red/ox ratio, which were 54.32 mU/mg and 0.51, respectively. The divergence of the reductive carboxylation activities and the red/ox ratios of heterotetrameric PFORs in hyperthermophilic archaea indicate the diversity of the functions of PFOR over long-term evolution. This can help us better understand the autotrophic CO2 fixation process in thermal vent, or in other CO2-rich high temperature habitat. (C) 2021 Elsevier Inc. All rights reserved.
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