ArticleJournal of bacteriology2008
A soluble NADH-dependent fumarate reductase in the reductive tricarboxylic acid cycle of Hydrogenobacter thermophilus TK-6.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
- Evidence for ecological adaptation of reductive citric acid and reverse oxidative citric acid cycles based on a survey of genomes from autotrophicFEMS microbes · 2026Review
- Impact of acetate on COISME communications · 2025Article
- In-Depth Computational Analysis of Natural and Artificial Carbon Fixation Pathways.Biodesign research · 2021Article
- Metabolic engineering of Aspergillus niger via ribonucleoprotein-based CRISPR-Cas9 system for succinic acid production from renewable biomass.Biotechnology for biofuels · 2020Article
- Preparation of stable recombinant Osm1 noncovalently bound with flavin adenosine dinucleotide cofactor for structural study.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Quantum chemistry reveals thermodynamic principles of redox biochemistry.PLoS computational biology · 2018Article
- A Rare Colonization in Peritoneum After Blunt Abdominal Trauma:Balkan medical journal · 2018Article
- Ecological aspects of the distribution of different autotrophic CO2 fixation pathways.Applied and environmental microbiology · 2011Review
- Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota.Journal of bacteriology · 2011Article
- Autotrophic carbon fixation in archaea.Nature reviews. Microbiology · 2010Review
- Carboxylation reaction catalyzed by 2-oxoglutarate:ferredoxin oxidoreductases from Hydrogenobacter thermophilus.Extremophiles : life under extreme conditions · 2010Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fumarate reductase (FRD) is an enzyme that reduces fumarate to succinate. In many organisms, it is bound to the membrane and uses electron donors such as quinol. In this study, an FRD from a thermophilic chemolithoautotrophic bacterium, Hydrogenobacter thermophilus TK-6, was purified and characterized. FRD activity using NADH as an electron donor was not detected in the membrane fraction but was found in the soluble fraction. The purified enzyme was demonstrated to be a novel type of FRD, consisting of five subunits. One subunit showed high sequence identity to the catalytic subunits of known FRDs. Although the genes of typical FRDs are assembled in a cluster, the five genes encoding the H. thermophilus FRD were distant from each other in the genome. Furthermore, phylogenetic analysis showed that the H. thermophilus FRD was located in a distinct position from those of known soluble FRDs. This is the first report of a soluble NADH-dependent FRD in Bacteria and of the purification of a FRD that operates in the reductive tricarboxylic acid cycle.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.