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Mapping the Initial Stages of a Protective Pathway that Enhances Catalytic Turnover by a Lytic Polysaccharide Monooxygenase.
Publication Type: Academic Journal
Source(s): Journal of the American Chemical Society [J Am Chem Soc] 2023 Sep 20; Vol. 145 (37), pp. 20672-20682. Date of Electronic Publication: 2023 Sep 09.
Abstract: Oxygenase and peroxygenase enzymes generate intermediates at their active sites which bring about the controlled functionalization of inert C-H bonds in substrates, such as in the enzymatic conversion of methane to methanol. To be viable catalysts, how...
Solution-State Inter-Copper Distribution of Redox Partner-Linked Copper Nitrite Reductases: A Pulsed Electron-Electron Double Resonance Spectroscopy Study.
Publication Type: Academic Journal
Source(s): The journal of physical chemistry letters [J Phys Chem Lett] 2022 Aug 04; Vol. 13 (30), pp. 6927-6934. Date of Electronic Publication: 2022 Jul 22.
Abstract: Copper nitrite reductases (CuNiRs) catalyze the reduction of nitrite to form nitric oxide. In recent years, new classes of redox partner linked CuNiRs have been isolated and characterized by crystallographic techniques. Solution-state biophysical studi...
Single crystal spectroscopy and multiple structures from one crystal (MSOX) define catalysis in copper nitrite reductases.
Publication Type: Academic Journal
Source(s): Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Jul 26; Vol. 119 (30), pp. e2205664119. Date of Electronic Publication: 2022 Jul 21.
Abstract: Many enzymes utilize redox-coupled centers for performing catalysis where these centers are used to control and regulate the transfer of electrons required for catalysis, whose untimely delivery can lead to a state incapable of binding the substrate, i...
Insights into the H 2 O 2 -driven catalytic mechanism of fungal lytic polysaccharide monooxygenases.
Publication Type: Academic Journal
Source(s): The FEBS journal [FEBS J] 2021 Jul; Vol. 288 (13), pp. 4115-4128. Date of Electronic Publication: 2021 Jan 26.
Abstract: Fungal lytic polysaccharide monooxygenases (LPMOs) depolymerise crystalline cellulose and hemicellulose, supporting the utilisation of lignocellulosic biomass as a feedstock for biorefinery and biomanufacturing processes. Recent investigations have sho...
Active Intermediates in Copper Nitrite Reductase Reactions Probed by a Cryotrapping-Electron Paramagnetic Resonance Approach.
Publication Type: Academic Journal
Source(s): Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2020 Aug 10; Vol. 59 (33), pp. 13936-13940. Date of Electronic Publication: 2020 Jun 04.
Abstract: Redox active metalloenzymes catalyse a range of biochemical processes essential for life. However, due to their complex reaction mechanisms, and often, their poor optical signals, detailed mechanistic understandings of them are limited. Here, we develo...
Radical-based photoinactivation of fatty acid photodecarboxylases.
Publication Type: Academic Journal
Source(s): Analytical biochemistry [Anal Biochem] 2020 Jul 01; Vol. 600, pp. 113749. Date of Electronic Publication: 2020 Apr 26.
Abstract: Fatty acid photodecarboxylases (FAP) are a recently discovered family of FAD-containing, light-activated enzymes, which convert fatty acids to n-alkanes/alkenes with potential applications in the manufacture of fine and speciality chemicals and fuels. ...
Photochemical Mechanism of Light-Driven Fatty Acid Photodecarboxylase.
Publication Type: Academic Journal
Source(s): ACS catalysis [ACS Catal] 2020 Jun 19; Vol. 10 (12), pp. 6691-6696. Date of Electronic Publication: 2020 May 19.
Abstract: Fatty acid photodecarboxylase (FAP) is a promising target for the production of biofuels and fine chemicals. It contains a flavin adenine dinucleotide cofactor and catalyzes the blue-light-dependent decarboxylation of fatty acids to generate the corres...
Protein Conformational Change Is Essential for Reductive Activation of Lytic Polysaccharide Monooxygenase by Cellobiose Dehydrogenase.
Publication Type: Academic Journal
Source(s): ACS catalysis [ACS Catal] 2020 May 01; Vol. 10 (9), pp. 4842-4853. Date of Electronic Publication: 2020 Mar 30.
Abstract: Large-scale protein domain dynamics and electron transfer are often associated. However, as protein motions span a broad range of time and length scales, it is often challenging to identify and thus link functionally relevant dynamic changes to electro...
Selectivity through discriminatory induced fit enables switching of NAD(P)H coenzyme specificity in Old Yellow Enzyme ene-reductases.
Publication Type: Academic Journal
Source(s): The FEBS journal [FEBS J] 2019 Aug; Vol. 286 (16), pp. 3117-3128. Date of Electronic Publication: 2019 May 13.
Abstract: Most ene-reductases belong to the Old Yellow Enzyme (OYE) family of flavin-dependent oxidoreductases. OYEs use nicotinamide coenzymes as hydride donors to catalyze the reduction of alkenes that contain an electron-withdrawing group. There have been man...
Unexpected Roles of a Tether Harboring a Tyrosine Gatekeeper Residue in Modular Nitrite Reductase Catalysis.
Publication Type: Academic Journal
Source(s): ACS catalysis [ACS Catal] 2019 Jul 05; Vol. 9 (7), pp. 6087-6099. Date of Electronic Publication: 2019 May 29.
Abstract: It is generally assumed that tethering enhances rates of electron harvesting and delivery to active sites in multidomain enzymes by proximity and sampling mechanisms. Here, we explore this idea in a tethered 3-domain, trimeric copper-containing nitrite...