Results 61 to 70 of about 39,076 (213)

The genetic basis of energy conservation in the sulfate-reducing bacterium Desulfovibrio alaskensis G20. [PDF]

open access: yes, 2014
Sulfate-reducing bacteria play major roles in the global carbon and sulfur cycles, but it remains unclear how reducing sulfate yields energy. To determine the genetic basis of energy conservation, we measured the fitness of thousands of pooled mutants of
Arkin, Adam P   +6 more
core   +1 more source

Nanozymes for Energy and Environmental Sustainability

open access: yesAdvanced Science, EarlyView.
At present, the widely used nanozymes are oxidoreductase and hydrolase, which have proved to have great application prospects in energy and environment. ABSTRACT Nanozymes have shown remarkable promise in addressing pressing challenges in energy and environmental sustainability.
Xiaoqi Li, Jinxing Chen, Shaojun Dong
wiley   +1 more source

“Candidatus Galacturonibacter soehngenii” Shows Acetogenic Catabolism of Galacturonic Acid but Lacks a Canonical Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase Complex

open access: yesFrontiers in Microbiology, 2020
Acetogens have the ability to fixate carbon during fermentation by employing the Wood-Ljungdahl pathway (WLP), which is highly conserved across Bacteria and Archaea.
Laura C. Valk   +7 more
doaj   +1 more source

Systematically Engineering for Efficient Production of 3‐Methyl‐1‐Butanol in Escherichia coli

open access: yesAdvanced Science, EarlyView.
An integrated metabolic engineering strategy was established for high‐level 3‐methyl‐1‐butanol biosynthesis in Escherichia coli. Molecular dynamics‐guided semi‐rational engineering of dihydroxyacid dehydratase uncovered and relieved key catalytic bottlenecks, while adaptive laboratory evolution enhanced strain robustness.
Nanfei Geng   +6 more
wiley   +1 more source

Properties of formate dehydrogenase in Methanobacterium formicicum [PDF]

open access: yesJournal of Bacteriology, 1982
Soluble formate dehydrogenase from Methanobacterium formicicum was purified 71-fold with a yield of 35%. Purification was performed anaerobically in the presence of 10 mM sodium azide which stabilized the enzyme. The purified enzyme reduced, with formate, 50 mumol of methyl viologen per min per mg of protein and 8.2 mumol of coenzyme F420 per min per ...
N L, Schauer, J G, Ferry
openaire   +2 more sources

Genome-Resolved Proteomic Stable Isotope Probing of Soil Microbial Communities Using 13CO2 and 13C-Methanol. [PDF]

open access: yes, 2019
Stable isotope probing (SIP) enables tracking the nutrient flows from isotopically labeled substrates to specific microorganisms in microbial communities. In proteomic SIP, labeled proteins synthesized by the microbial consumers of labeled substrates are
Banfield, Jillian F   +10 more
core   +1 more source

EDTA‐Functionalized Nanoscale Metal–Organic Framework for Onco‐Cardiology via Radiochemotherapy Synergy and Spatiotemporally Matched Iron Chelation

open access: yesAdvanced Science, EarlyView.
Doxorubicin (DOX)‐induced cardiotoxicity is a major limitation to its broader clinical application, while cardioprotective interventions often risk reducing the anticancer efficacy of DOX. To address these challenges, this work constructs an EDTA‐functionalized metal–organic framework that enhances tumor therapy and provides efficient cardioprotection ...
Daojing Yuan   +8 more
wiley   +1 more source

Mechanism of Action of Formate Dehydrogenases [PDF]

open access: yesJournal of the American Chemical Society
The molybdenum- and tungsten-containing formate dehydrogenases from a variety of microorganisms catalyze the reversible interconversion of formate and CO2; several, in fact, function as CO2 reductases in the reverse direction under physiological conditions.
Dimitri Niks   +4 more
openaire   +3 more sources

Crystal structure of NAD‐dependent formate dehydrogenase [PDF]

open access: yesEuropean Journal of Biochemistry, 1992
The ternary complex of NAD‐dependent formate dehydrogenase (FDH) from the methylotrophic bacterium Pseudomonas sp. 101 (enzyme‐NAD‐azide) has been crystallised in the space group P212121 with cell dimensions a = 11.60 nm, b= 11.33 nm, c= 6.34 nm. There is 1 dimeric molecule/asymmetric unit.
V S, Lamzin   +6 more
openaire   +2 more sources

One-carbon metabolism in cancer [PDF]

open access: yes, 2017
Cells require one-carbon units for nucleotide synthesis, methylation and reductive metabolism, and these pathways support the high proliferative rate of cancer cells.
AJ MacFarlane   +55 more
core   +1 more source

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