Direct Electron Transfer between the frhAGB-Encoded Hydrogenase and Thioredoxin Reductase in the Nonmethanogenic Archaeon Thermococcus onnurineus NA1 SCIE SCOPUS

Cited 1 time in WEB OF SCIENCE Cited 0 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)
Jung, Hae Chang(정해창)Kang, Sung Gyun(강성균)Lee, Hyun Sook(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
Subject
H-2 PRODUCTION; SULFUR METABOLISM; SEQUENCE; CLONING; PURIFICATION; EXPRESSION; PROTEIN; NICKEL; SURR
Keywords
F-420-reducing hydrogenase; thioredoxin reductase; direct electron transfer; frhAGB-encoded hydrogenase; protein-protein interaction
Type
Article
Language
English
Document Type
Article
Publisher
AMER SOC MICROBIOLOGY
Related Researcher
Research Interests

Microbial biotechnology,Marine enzymes,미생물 활용,효소 개발

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