Direct Electron Transfer between the frhAGB-Encoded Hydrogenase and Thioredoxin Reductase in the Nonmethanogenic Archaeon Thermococcus onnurineus NA1
SCIE
SCOPUS
Cited 6 time in
WEB OF SCIENCE
Cited 6 time in
Scopus
-
Title
- Direct Electron Transfer between the frhAGB-Encoded Hydrogenase and Thioredoxin Reductase in the Nonmethanogenic Archaeon Thermococcus onnurineus NA1
-
Author(s)
- Jung, Hae-Chang; Lim, Jae Kyu; Yang, Tae-Jun; Kang, Sung Gyun; Lee, Hyun Sook
- KIOST Author(s)
- Lim, Jae Kyu(임재규); Kang, Sung Gyun(강성균); Lee, Hyun Sook(이현숙)
-
Alternative Author(s)
- 정해창; 임재규; 양태준; 강성균; 이현숙
-
Publication Year
- 2020-03
-
Abstract
- To date, NAD(P)H, ferredoxin, and coenzyme F-420 have been identified as electron donors for thioredoxin reductase (TrxR). In this study, we present a novel electron source for TrxR. In the hyperthermophilic archaeon Thermococcus onnurineus NA1, the frhAGB-encoded hydrogenase, a homolog of the F-420- reducing hydrogenase of methanogens, was demonstrated to interact with TrxR in coimmuno-precipitation experiments and in vitro pulldown assays. Electrons derived from H-2 oxidation by the frhAGB-encoded hydrogenase were transferred to TrxR and reduced Pdo, a redox partner of TrxR. Interaction and electron transfer were observed between TrxR and the heterodimeric hydrogenase complex (FrhAG) as well as the heterotrimeric complex (FrhAGB). Hydrogen-dependent reduction of TrxR was 7-fold less efficient than when NADPH was the electron donor. This study not only presents a different type of electron donor for TrxR but also reveals new functionality of the frhAGB-encoded hydrogenase utilizing a protein as an electron acceptor. IMPORTANCE This study has importance in that TrxR can use H-2 as an electron donor with the aid of the frhAGB-encoded hydrogenase as well as NAD(P)H in T. onnurineus NA1. Further studies are needed to explore the physiological significance of this protein. This study also has importance as a significant step toward understanding the functionality of the frhAGB-encoded hydrogenase in a nonmethanogen; the hydrogenase can transfer electrons derived from oxidation of H-2 to a protein target by direct contact without the involvement of an electron carrier, which is distinct from the mechanism of its homologs, F-420-reducing hydrogenases of methanogens.
-
ISSN
- 0099-2240
-
URI
- https://sciwatch.kiost.ac.kr/handle/2020.kiost/38730
-
DOI
- 10.1128/AEM.02630-19
-
Bibliographic Citation
- APPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.86, no.6, 2020
-
Publisher
- AMER SOC MICROBIOLOGY
-
Keywords
- F-420-reducing hydrogenase; thioredoxin reductase; direct electron transfer; frhAGB-encoded hydrogenase; protein-protein interaction
-
Type
- Article
-
Language
- English
-
Document Type
- Article
- Files in This Item:
-
There are no files associated with this item.
Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.