Formate oxidase of Aspergillus oryzae RIB40 contains an 8-replaced FAD with molecular mass of 799 as cofactor. The ¹H-NMR spectrum of the cofactor fraction obtained from the enzyme indicated that the 8-replaced FAD in the fraction was 8-formyl-FAD, present in open form and hemiacetal form. The oxidation-reduction potentials of the open and hemiacetal forms were estimated by cyclic voltammetry to be -47 and -177 mV vs. Normal Hydrogen Electrode respectively. The structure of the enzyme was constructed using diffraction data to 2.24 Å resolution collected from a crystal of the enzyme. His₅₁₁ and Arg₅₅₄ were situated close to the pyrimidine part of the isoalloxazine ring of 8-formyl-FAD in open form. The enzyme had 8-formyl-FAD, the oxidation potential of which was approximately 160 mV more positive than that of FAD, and the His-Arg pair at the catalytic site, unlike the other enzymes belonging to the glucose-methanol-choline oxidoreductase family.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1271/bbb.110153 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Hybrid Enzyme-Electrocatalyst Cascade Modified Gas-diffusion Electrodes for Methanol Formation from Carbon Dioxide.
Angew Chem Int Ed Engl
December 2024
Ruhr University Bochum, Analytische Chemie, Universitätsstr 150, 44780, Bochum, GERMANY.
We propose a hybrid electrocatalytic-bioelectrocatalytic reaction cascade integrated on a gas diffusion electrode for CO2 reduction under selective formation of methanol. Ag-Bi2O3 selectively reduces gaseous CO2 to formate at neutral pH conditions. A subsequent enzymatic cascade comprising formaldehyde dehydro-genase and alcohol dehydrogenase, which are both nicotinamide adenine dinucleotide (NAD)-dependent, further reduce formate sequentially to formaldehyde and methanol.
View Article and Find Full Text PDFHarnessing Ruthenium and Copper Catalysts for Formate Dehydrogenase Reactions.
Chem Rec
December 2024
Artificial Photosynthesis Laboratory, Science Block, Department of Chemistry and Chemical Biology, Indian Institute of Technology (Indian School of Mines) Dhanbad, Jharkhand, 826004, India.
Formic acid (HCOOH) is a promising source of hydrogen energy that can be used to produce hydrogen in a more economical and ecological way. Formic acid is a simple carboxylic acid with a high hydrogen concentration and is generally stable, making it useful as a hydrogen transporter. Catalytic dehydrogenation is usually used to extract hydrogen from formic acid; this process releases hydrogen gas and yields carbon dioxide as a byproduct.
View Article and Find Full Text PDFEfficient bioelectrocatalytic NADH regeneration with a novel amino-functionalized viologen redox polymer.
Bioelectrochemistry
April 2025
Instituto de Catálisis y Petroleoquímica, CSIC, C/Marie Curie 2, 28049 Madrid, Spain. Electronic address:
Article Synopsis
- Oxidoreductase enzymes, important in organic synthesis and pharmaceuticals, rely on NADH for reactions, creating a need for cost-effective NADH regeneration methods.
- This study introduces a new amino-functionalized viologen that, when combined with diaphorase, effectively generates bioactive NADH with high selectivity and efficiency.
- Testing revealed that this system significantly enhanced formate production compared to traditional methods, highlighting its potential for sustainable NADH regeneration at low energy requirements.
All-in-One CO Capture and Transformation: Lessons from Formylmethanofuran Dehydrogenases.
Acc Chem Res
December 2024
Max Planck Institute for Marine Microbiology, Celsiusstraße 1, 28359 Bremen, Germany.
Article Synopsis
- Carbon-one-unit (C1) feedstocks like formate and formamide are important for producing organic molecules, and they're cleaner alternatives to carbon monoxide from fossil fuels.
- New methods are emerging to transform carbon dioxide (CO), a greenhouse gas, into these valuable feedstocks, addressing the need for carbon recycling and sustainability.
- The formylmethanofuran dehydrogenase (FMD) enzyme, found in certain archaea, effectively captures and processes CO without high energy costs, playing a crucial role in the carbon cycle and potentially aiding in renewable energy solutions.
Molybdenum-containing CO dehydrogenase and formate dehydrogenases.
Methods Enzymol
November 2024
Department of Biochemistry, University of California, Riverside, CA, United States. Electronic address:
The molybdenum-containing CO dehydrogenase and the formate dehydrogenases catalyze important interconversions of one-carbon compounds, the former oxidizing CO to CO, and the latter the reversible interconversion of CO and formate. Methodologies to study these two enzymes are discussed.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!