Lignin induced iron reduction by novel sp., Tolumonas lignolytic BRL6-1

Autor: Carrie D. Nicora, Young-Mo Kim, Rosalie K. Chu, Andrew F. Billings, Lani DeDiego, Kristen M. DeAngelis, Joshua N. Adkins, Blake A. Simmons, Roberto Orellana, Gina Chaput
Přispěvatelé: Cullen, Daniel
Jazyk: angličtina
Rok vydání: 2020
Předmět:
Metabolic Processes
Protein Folding
Lignin
Biochemistry
chemistry.chemical_compound
Electrochemistry
Macromolecular Structure Analysis
Metabolites
Biomass
Protein Metabolism
Gel Electrophoresis
chemistry.chemical_classification
Staining
0303 health sciences
Multidisciplinary
biology
Chemical Reactions
food and beverages
Chemistry
Physical Sciences
Medicine
Anaerobic bacteria
Sulfatases
Radical SAM
Oxidation-Reduction
Glycolysis
Peroxidase
Research Article
Protein Structure
Silver Staining
food.ingredient
General Science & Technology
Science
Radical
Iron
macromolecular substances
Anaerobic Bacteria
Electrophoretic Staining
Research and Analysis Methods
complex mixtures
Aeromonadaceae
03 medical and health sciences
Electrophoretic Techniques
food
Bacterial Proteins
Cellulose
Molecular Biology
030304 developmental biology
Bacteria
030306 microbiology
fungi
technology
industry
and agriculture

Chemical Compounds
Organisms
Biology and Life Sciences
Proteins
Enzyme
Metabolism
chemistry
Specimen Preparation and Treatment
Tolumonas
biology.protein
Oxidation-Reduction Reactions
Zdroj: PLoS ONE
PloS one, vol 15, iss 9
PLoS ONE, Vol 15, Iss 9, p e0233823 (2020)
ISSN: 1932-6203
Popis: Lignin is the second most abundant carbon polymer on earth and despite having more fuel value than cellulose, it currently is considered a waste byproduct in many industrial lignocellulose applications. Valorization of lignin relies on effective and green methods of de-lignification, with a growing interest in the use of microbes. Here we investigate the physiology and molecular response of the novel facultative anaerobic bacterium, Tolumonas lignolytica BRL6-1, to lignin under anoxic conditions. Physiological and biochemical changes were compared between cells grown anaerobically in either lignin-amended or unamended conditions. In the presence of lignin, BRL6-1 accumulates higher biomass and has a shorter lag phase compared to unamended conditions, and 14% of the proteins determined to be significantly higher in abundance by log2 fold-change of 2 or greater were related to Fe(II) transport in late logarithmic phase. Ferrozine assays of the supernatant confirmed that Fe(III) was bound to lignin and reduced to Fe(II) only in the presence of BRL6-1, suggesting redox activity by the cells. LC-MS/MS analysis of the secretome showed an extra band at 20 kDa in lignin-amended conditions. Protein sequencing of this band identified a protein of unknown function with homology to enzymes in the radical SAM superfamily. Expression of this protein in lignin-amended conditions suggests its role in radical formation. From our findings, we suggest that BRL6-1 is using a protein in the radical SAM superfamily to interact with the Fe(III) bound to lignin and reducing it to Fe(II) for cellular use, increasing BRL6-1 yield under lignin-amended conditions. This interaction potentially generates organic free radicals and causes a radical cascade which could modify and depolymerize lignin. Further research should clarify the extent to which this mechanism is similar to previously described aerobic chelator-mediated Fenton chemistry or radical producing lignolytic enzymes, such as lignin peroxidases, but under anoxic conditions.
Databáze: OpenAIRE