ArticleThe Journal of biological chemistry2016
Heterogeneity in the Histidine-brace Copper Coordination Sphere in Auxiliary Activity Family 10 (AA10) Lytic Polysaccharide Monooxygenases.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 57 citations in OpenAlex.
- Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO).Nature communications · 2024Article
- Enhancing enzymatic saccharification yields of cellulose at high solid loadings by combining different LPMO activities.Biotechnology for biofuels and bioproducts · 2024Article
- A novel starch-active lytic polysaccharide monooxygenase discovered with bioinformatics screening and its application in textile desizing.BMC biotechnology · 2024Article
- TheApplied and environmental microbiology · 2023Article
- Perdeuterated GbpA Enables Neutron Scattering Experiments of a Lytic Polysaccharide Monooxygenase.ACS omega · 2023Article
- Chitin Biodegradation by Lytic Polysaccharide Monooxygenases fromInternational journal of molecular sciences · 2022Article
- Orchestrating copper binding: structure and variations on the cupredoxin fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Chitin-Active Lytic Polysaccharide Monooxygenases Are Rare inApplied and environmental microbiology · 2022Article
- Decoding the Ambiguous Electron Paramagnetic Resonance Signals in the Lytic Polysaccharide Monooxygenase fromInorganic chemistry · 2022Article
- Role for a Lytic Polysaccharide Monooxygenase in Cell Wall Remodeling in Streptomyces coelicolor.mBio · 2022Article
- Activity and substrate specificity of lytic polysaccharide monooxygenases: An ATR FTIR-based sensitive assay tested on a novel species from Pseudomonas putida.Protein science : a publication of the Protein Society · 2022Article
- Molecular analysis of genes involved in chitin degradation from the chitinolytic bacterium Bacillus velezensis.Antonie van Leeuwenhoek · 2022Article
- Kinetic insights into the role of the reductant in HThe Journal of biological chemistry · 2019Article
- Profile Comparer Extended: phylogeny of lytic polysaccharide monooxygenase families using profile hidden Markov model alignments.F1000Research · 2019Article
- On the functional characterization of lytic polysaccharide monooxygenases (LPMOs).Biotechnology for biofuels · 2019Review
- Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function.Chemical reviews · 2018Review
- Methylation of the N-terminal histidine protects a lytic polysaccharide monooxygenase from auto-oxidative inactivation.Protein science : a publication of the Protein Society · 2018Article
- Oxygen Activation by Cu LPMOs in Recalcitrant Carbohydrate Polysaccharide Conversion to Monomer Sugars.Chemical reviews · 2018Review
- The discovery of novel LPMO families with a new Hidden Markov model.BMC research notes · 2017Article
- Lytic polysaccharide monooxygenases: a crystallographer's view on a new class of biomass-degrading enzymes.IUCrJ · 2016Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Copper-dependent lytic polysaccharide monooxygenases (LPMOs) are enzymes that oxidatively deconstruct polysaccharides. The active site copper in LPMOs is coordinated by a histidine-brace. This utilizes the amino group and side chain of the N-terminal His residue with the side chain of a second His residue to create a T-shaped arrangement of nitrogen ligands. We report a structural, kinetic, and thermodynamic appraisal of copper binding to the histidine-brace in an auxiliary activity family 10 (AA10) LPMO from Streptomyces lividans (SliLPMO10E). Unexpectedly, we discovered the existence of two apo-SliLPMO10E species in solution that can each bind copper at a single site with distinct kinetic and thermodynamic (exothermic and endothermic) properties. The experimental EPR spectrum of copper-bound SliLPMO10E requires the simulation of two different line shapes, implying two different copper-bound species, indicative of three and two nitrogen ligands coordinating the copper. Amino group coordination was probed through the creation of an N-terminal extension variant (SliLPMO10E-Ext). The kinetics and thermodynamics of copper binding to SliLPMO10E-Ext are in accord with copper binding to one of the apo-forms in the wild-type protein, suggesting that amino group coordination is absent in the two-nitrogen coordinate form of SliLPMO10E. Copper binding to SliLPMO10B was also investigated, and again it revealed the presence of two apo-forms with kinetics and stoichiometry of copper binding identical to that of SliLPMO10E. Our findings highlight that heterogeneity exists in the active site copper coordination sphere of LPMOs that may have implications for the mechanism of loading copper in the cell.
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