Results 41 to 50 of about 850,773 (307)

Adatoms and nanoengineering of carbon

open access: yes, 2001
We present a new and general mechanism for inter-conversion of carbon structures via a catalytic exchange process, which operates under conditions of Frenkel pair generation.
Austin   +26 more
core   +2 more sources

The Catalytic Mechanism of Carbonic Anhydrase [PDF]

open access: yesProceedings of the National Academy of Sciences, 1973
It is shown that an “inverse” relationship between the pH dependencies of the rates of hydration of CO 2 and dehydration of HCO 3 - by carbonic anhydrase (EC 4.2.1.1) is a direct consequence of the thermodynamic equilibrium between CO 2 and HCO ...
S, Lindskog, J E, Coleman
openaire   +2 more sources

Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?

open access: yesFEBS Letters, EarlyView.
This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes   +3 more
wiley   +1 more source

Microbial (E)-4-hydroxy-3-methylbut-2-enyl pyrophosphate reductase (IspH) and its biotechnological potential: A mini review

open access: yesFrontiers in Bioengineering and Biotechnology, 2022
(E)-4-hydroxy-3-methylbut-2-enyl pyrophosphate (HMBPP) reductase (IspH) is a [4Fe-4S] cluster-containing enzyme, involved in isoprenoid biosynthesis as the final enzyme of the methylerythritol phosphate (MEP) pathway found in many bacteria and malaria ...
Shiyong Huang   +4 more
doaj   +1 more source

Unraveling the Catalytic Mechanism of Nitrile Hydratases [PDF]

open access: yes, 2007
To elucidate a detailed catalytic mechanism for nitrile hydratases (NHases), the pH and temperature dependence of the kinetic constants kcat and Km for the cobalt-type NHase from Pseudonocardia thermophila JCM 3095 (PtNHase) were examined.
Holz, Richard C., Mitra, Sanghamitra
core   +1 more source

New aspects of the electrochemical-catalytic (EC’) mechanism in square-wave voltammetry [PDF]

open access: yes, 2015
Several new theoretical aspects of the electrocatalytic (regenerative) EC’ mechanism under conditions of square-wave (SWV) and staircase cyclic voltammetry (SCV) are presented.
Gulaboski, Rubin, Mirceski, Valentin
core   +1 more source

The catalytic mechanism of sulfoxide synthases

open access: yesCurrent Opinion in Chemical Biology, 2020
Sulfoxide synthases are non-heme iron enzymes that catalyze oxidative carbonsulfur bond formation in the biosynthesis of thiohistidines such as ergothioneine and ovothiol. The catalytic mechanism of these enzymes has been studied by protein crystallography, steady-state kinetics, non-natural amino acid incorporation and computational modeling.
Anja R. Stampfli, Florian P. Seebeck
openaire   +3 more sources

Structural insights into lacto‐N‐biose I recognition by a family 32 carbohydrate‐binding module from Bifidobacterium bifidum

open access: yesFEBS Letters, EarlyView.
Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang   +5 more
wiley   +1 more source

Copper Modulated Lead‐Free Cs4MnSb2Cl12 Double Perovskite Microcrystals for Photocatalytic Reduction of CO2

open access: yesAdvanced Science
In order to deal with the global energy crisis and environmental problems, reducing carbon dioxide through artificial photosynthesis has become a hot topic.
Bo Gao   +11 more
doaj   +1 more source

Boron carboxylate catalysis of homoallylboration. [PDF]

open access: yes, 2014
Boron tris(trifluoroacetate) is identified as the first effective catalyst for the homoallyl- and homocrotylboration of aldehydes by cyclopropylcarbinylboronates.
Dugas, Gabrielle J   +3 more
core  

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