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http://dx.doi.org/10.1002/anie.201208738 | DOI Listing |
Proc Natl Acad Sci U S A
January 2025
Department of Biochemistry, Brandeis University, Waltham, MA 02454.
Reversible protein phosphorylation directs essential cellular processes including cell division, cell growth, cell death, inflammation, and differentiation. Because protein phosphorylation drives diverse diseases, kinases and phosphatases have been targets for drug discovery, with some achieving remarkable clinical success. Most protein kinases are activated by phosphorylation of their activation loops, which shifts the conformational equilibrium of the kinase toward the active state.
View Article and Find Full Text PDFNat Commun
December 2024
Center of Artificial Photosynthesis for Solar Fuels and Department of Chemistry, School of Science, Westlake University, Hangzhou, China.
Natural enzymes feature distinctive second spheres near their active sites, leading to exquisite catalytic reactivity. However, incumbent synthetic strategies offer limited versatility in functionalizing the second spheres of heterogeneous catalysts. Here, we prepare an enzyme-mimetic single Co-N atom catalyst with an elaborately configured pendant amine group in the second sphere via 1,3-dipolar cycloaddition, which switches the oxygen reduction reaction selectivity from the 4e to the 2e pathway under acidic conditions.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
December 2024
Qingdao University of Science and Technology, State Key Laboratory Base of Eco-Chemical Engineering College of Chemical Engineering, Qingdao, CHINA.
Electrocatalytic reduction of NO3- is a green and sustainable method that not only helps to treat industrial pollutants in wastewater, but also produces valuable chemicals. However, the slow dynamics of the proton-coupled electron transfer process results in a high barrier and low conversion efficiency. In this work, the Se-deficient FeSe2/Fe3O4 heterojunction was synthesized, which showed excellent electrochemical performance in 0.
View Article and Find Full Text PDFPlant Physiol Biochem
December 2024
Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu, 610213, China. Electronic address:
Cytochrome P450 enzymes (CYPs), the members of the largest superfamily of enzymes in plant kingdom, catalyze a variety of functional group transformations involved in metabolite biosynthesis, end-product derivatization, and exogeneous molecule detoxification. Nevertheless, CYPs' functional characterization and practically industrial application have been largely encumbered by their critical dependency on the reducing equivalent for the catalytic cycling, driven by the tedious electron relay mediated by CYP reductase (CPR). Here, we report a photoinduced electron transfer system that initiates and sustains the CYP-catalyzed reaction cycling.
View Article and Find Full Text PDFJ Biol Chem
December 2024
Institute of Molecular Biology Department of Chemistry and Biochemistry 1229 University of Oregon Eugene, OR 97403. Electronic address:
The Par complex polarizes the plasma membrane of diverse animal cells using the catalytic activity of atypical Protein Kinase C (aPKC) to pattern substrates. Two upstream regulators of the Par complex, Cdc42 and Par-3, bind separately to the complex to influence its activity in different ways. Each regulator binds a distinct member of the complex, Cdc42 to Par-6 and Par-3 to aPKC, making it unclear how they influence one another's binding.
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