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Yoshiyuki Nomura - One of the best experts on this subject based on the ideXlab platform.
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gfsa encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of o glycan in aspergillus nidulans and aspergillus fumigatus
Molecular Microbiology, 2013Co-Authors: Yuji Komachi, Haruka Motomatsu, Karina Kizjakina, Shintaro Hatakeyama, Keisuke Ekino, Taiki Futagami, Kaoru Takegawa, Pablo Sobrado, Masatoshi Goto, Yoshiyuki NomuraAbstract:The cell walls of filamentous fungi in the genus Aspergillus have galactofuranose-containing polysaccharides and glycoconjugates, including O-glycans, N-glycans, fungal-type galactomannan, and glycosylinositolphosphoceramide, which are important for cell wall integrity. Here, we attempted to identify galactofuranosyltransferases that couple galactofuranose monomers onto other wall components in Aspergillus nidulans. Using reverse-genetic and biochemical approaches, we identified that the AN8677 gene encoded a galactofuranosyltransferase, which we called GfsA, involved in galactofuranose (Galf) antigen biosynthesis. Disruption of gfsA reduced binding of β-Galf-specific antibody EB-A2 to O-glycosylated WscA protein and galactomannoproteins. The results of an in-vitro galactofuranose antigen synthase assay revealed that GfsA has β1,5- or β1,6- galactofuranosyltransferase activity for O-glycans in glycoproteins, uses UDP-D-galactofuranose as a sugar donor, and requires a divalent Manganese Cation for activity. GfsA was found to be localized at the Golgi apparatus based on cellular fractionation experiments. ΔgfsA cells exhibited an abnormal morphology characterized by poor hyphal extension, hyphal curvature, and limited formation of conidia. Several gfsA orthologs were identified in members of the Pezizomycotina subphylum of Ascomycota, including the human pathogen Aspergillus fumigatus. To our knowledge, this is the first characterization of a fungal β-galactofuranosyltransferase, which was shown to be involved in galactofuranose antigen biosynthesis of O-glycans in the Golgi.
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gfsA encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of O-glycan in Aspergillus nidulans and Aspergillus fumigatus
Molecular Microbiology, 2013Co-Authors: Yuji Komachi, Haruka Motomatsu, Karina Kizjakina, Shintaro Hatakeyama, Keisuke Ekino, Taiki Futagami, Kaoru Takegawa, Pablo Sobrado, Masatoshi Goto, Yoshiyuki NomuraAbstract:The cells walls of filamentous fungi in the genus Aspergillus have galactofuranose (Galf)-containing polysaccharides and glycoconjugates, including O-glycans, N-glycans, fungal-type galactomannan and glycosylinositolphosphoceramide, which are important for cell wall integrity. Here, we attempted to identify galactofuranosyltransferases that couple Galf monomers onto other wall components in Aspergillus nidulans. Using reverse-genetic and biochemical approaches, we identified that the AN8677 gene encoded a galactofuranosyltransferase, which we called GfsA, involved in Galf antigen biosynthesis. Disruption of gfsA reduced binding of β-Galf-specific antibody EB-A2 to O-glycosylated WscA protein and galactomannoproteins. The results of an in-vitro Galf antigen synthase assay revealed that GfsA has β1,5- or β1,6-galactofuranosyltransferase activity for O-glycans in glycoproteins, uses UDP-d-Galf as a sugar donor, and requires a divalent Manganese Cation for activity. GfsA was found to be localized at the Golgi apparatus based on cellular fractionation experiments. ΔgfsA cells exhibited an abnormal morphology characterized by poor hyphal extension, hyphal curvature and limited formation of conidia. Several gfsA orthologues were identified in members of the Pezizomycotina subphylum of Ascomycota, including the human pathogen Aspergillus fumigatus. To our knowledge, this is the first characterization of a fungal β-galactofuranosyltransferase, which was shown to be involved in Galf antigen biosynthesis of O-glycans in the Golgi.
Ion C Halalay - One of the best experts on this subject based on the ideXlab platform.
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on the oxidation state of Manganese ions in li ion battery electrolyte solutions
Journal of the American Chemical Society, 2017Co-Authors: Anjan Banerjee, Doron Aurbach, Yuliya Shilina, Baruch Ziv, Joseph M Ziegelbauer, Shalom Luski, Ion C HalalayAbstract:We demonstrate herein that Mn3+ and not Mn2+, as commonly accepted, is the dominant dissolved Manganese Cation in LiPF6-based electrolyte solutions of Li-ion batteries with lithium manganate spinel positive and graphite negative electrodes chemistry. The Mn3+ fractions in solution, derived from a combined analysis of electron paramagnetic resonance and inductively coupled plasma spectroscopy data, are ∼80% for either fully discharged (3.0 V hold) or fully charged (4.2 V hold) cells, and ∼60% for galvanostatically cycled cells. These findings agree with the average oxidation state of dissolved Mn ions determined from X-ray absorption near-edge spectroscopy data, as verified through a speciation diagram analysis. We also show that the fractions of Mn3+ in the aprotic nonaqueous electrolyte solution are constant over the duration of our experiments and that disproportionation of Mn3+ occurs at a very slow rate.
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On the Oxidation State of Manganese Ions in Li-Ion Battery Electrolyte Solutions
2017Co-Authors: Anjan Banerjee, Doron Aurbach, Yuliya Shilina, Baruch Ziv, Joseph M Ziegelbauer, Shalom Luski, Ion C HalalayAbstract:We demonstrate herein that Mn3+ and not Mn2+, as commonly accepted, is the dominant dissolved Manganese Cation in LiPF6-based electrolyte solutions of Li-ion batteries with lithium manganate spinel positive and graphite negative electrodes chemistry. The Mn3+ fractions in solution, derived from a combined analysis of electron paramagnetic resonance and inductively coupled plasma spectroscopy data, are ∼80% for either fully discharged (3.0 V hold) or fully charged (4.2 V hold) cells, and ∼60% for galvanostatically cycled cells. These findings agree with the average oxidation state of dissolved Mn ions determined from X-ray absorption near-edge spectroscopy data, as verified through a speciation diagram analysis. We also show that the fractions of Mn3+ in the aprotic nonaqueous electrolyte solution are constant over the duration of our experiments and that disproportionation of Mn3+ occurs at a very slow rate
Yuji Komachi - One of the best experts on this subject based on the ideXlab platform.
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gfsa encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of o glycan in aspergillus nidulans and aspergillus fumigatus
Molecular Microbiology, 2013Co-Authors: Yuji Komachi, Haruka Motomatsu, Karina Kizjakina, Shintaro Hatakeyama, Keisuke Ekino, Taiki Futagami, Kaoru Takegawa, Pablo Sobrado, Masatoshi Goto, Yoshiyuki NomuraAbstract:The cell walls of filamentous fungi in the genus Aspergillus have galactofuranose-containing polysaccharides and glycoconjugates, including O-glycans, N-glycans, fungal-type galactomannan, and glycosylinositolphosphoceramide, which are important for cell wall integrity. Here, we attempted to identify galactofuranosyltransferases that couple galactofuranose monomers onto other wall components in Aspergillus nidulans. Using reverse-genetic and biochemical approaches, we identified that the AN8677 gene encoded a galactofuranosyltransferase, which we called GfsA, involved in galactofuranose (Galf) antigen biosynthesis. Disruption of gfsA reduced binding of β-Galf-specific antibody EB-A2 to O-glycosylated WscA protein and galactomannoproteins. The results of an in-vitro galactofuranose antigen synthase assay revealed that GfsA has β1,5- or β1,6- galactofuranosyltransferase activity for O-glycans in glycoproteins, uses UDP-D-galactofuranose as a sugar donor, and requires a divalent Manganese Cation for activity. GfsA was found to be localized at the Golgi apparatus based on cellular fractionation experiments. ΔgfsA cells exhibited an abnormal morphology characterized by poor hyphal extension, hyphal curvature, and limited formation of conidia. Several gfsA orthologs were identified in members of the Pezizomycotina subphylum of Ascomycota, including the human pathogen Aspergillus fumigatus. To our knowledge, this is the first characterization of a fungal β-galactofuranosyltransferase, which was shown to be involved in galactofuranose antigen biosynthesis of O-glycans in the Golgi.
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gfsA encodes a novel galactofuranosyltransferase involved in biosynthesis of galactofuranose antigen of O-glycan in Aspergillus nidulans and Aspergillus fumigatus
Molecular Microbiology, 2013Co-Authors: Yuji Komachi, Haruka Motomatsu, Karina Kizjakina, Shintaro Hatakeyama, Keisuke Ekino, Taiki Futagami, Kaoru Takegawa, Pablo Sobrado, Masatoshi Goto, Yoshiyuki NomuraAbstract:The cells walls of filamentous fungi in the genus Aspergillus have galactofuranose (Galf)-containing polysaccharides and glycoconjugates, including O-glycans, N-glycans, fungal-type galactomannan and glycosylinositolphosphoceramide, which are important for cell wall integrity. Here, we attempted to identify galactofuranosyltransferases that couple Galf monomers onto other wall components in Aspergillus nidulans. Using reverse-genetic and biochemical approaches, we identified that the AN8677 gene encoded a galactofuranosyltransferase, which we called GfsA, involved in Galf antigen biosynthesis. Disruption of gfsA reduced binding of β-Galf-specific antibody EB-A2 to O-glycosylated WscA protein and galactomannoproteins. The results of an in-vitro Galf antigen synthase assay revealed that GfsA has β1,5- or β1,6-galactofuranosyltransferase activity for O-glycans in glycoproteins, uses UDP-d-Galf as a sugar donor, and requires a divalent Manganese Cation for activity. GfsA was found to be localized at the Golgi apparatus based on cellular fractionation experiments. ΔgfsA cells exhibited an abnormal morphology characterized by poor hyphal extension, hyphal curvature and limited formation of conidia. Several gfsA orthologues were identified in members of the Pezizomycotina subphylum of Ascomycota, including the human pathogen Aspergillus fumigatus. To our knowledge, this is the first characterization of a fungal β-galactofuranosyltransferase, which was shown to be involved in Galf antigen biosynthesis of O-glycans in the Golgi.
Diss Loïc - One of the best experts on this subject based on the ideXlab platform.
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Fungal Manganese transporters: diversity and functional analysis in the saprophytic fungus Phanerochaete chrysosporium
2012Co-Authors: Diss LoïcAbstract:P. chrysosporium est un champignon saprophyte capable de dégrader de nombreux xénobiotiques, ce qui le rend particulièrement intéressant pour des appliCations en bioremédiation. Plusieurs publiCations mettent en avant l'importance de la maîtrise de l'homéostasie métallique dans la production de certaines enzymes lignolytiques. La présence de manganèse est en effet nécessaire à la production des manganèses peroxydases, alors qu'à l'inverse une carence permettra la production de lignines peroxydases. Cependant, la caractérisation de transporteurs impliqués dans le contrôle de l'homéostasie métallique n'a fait l'objet de recherches poussées que chez le champignon modèle S. cerevisiae. L'analyse des transporteurs putatifs de manganèse de 26 espèces fongiques représentant 20 ordres fongiques a permis de constituer un répertoire de 281 transporteurs de manganèse. L'analyse phylogénétique a permis de mettre en évidence que des processus de dupliCation, mais également de délétion, avaient eu lieu en particulier chez S. cerevisiae. Cependant ce dernier ne possède pas de transporteurs de manganèse appartenant à la famille des Cation Diffusion Facilitator. Dans le génome de P. chrysosporium, onze transporteurs de manganèse appartenant à différentes familles de gènes ont été identifiés. Le niveau d'expression de ces différents gènes a été étudié notamment en condition lignolytique. Ces transporteurs ont également été clonés afin de vérifier leurs fonctions par complémentation en système hétérologue. Cette étude a permis de mettre en évidence les transporteurs de manganèse putatifs de nombreux organismes fongiques, ainsi que l'absence d'une famille de transporteurs impliquée dans les mouvements de manganèse chez S. cerevisiaeP. chrysosporium is a saprophytic fungus able to degrade many xenobiotics which makes it particularly attractive for appliCations in bioremediation. Several publiCations highlight the importance of metal homeostasis in the production of lignolytics enzymes. Indeed the presence of Manganese is required for the production of Manganese peroxidase. Conversely, deficiency allows the production of lignins peroxidases. Characterization of transporters involved in the control of Manganese homeostasis has been only researched in the model S. cerevisiae. Analysis of putative Manganese transporters of 26 fungal species representing 20 orders of fungus was used to form a repertory of 281 transporters of Manganese. Phylogenetic analysis allowed to highlight that dupliCation process, but also deletion, had occurred particularly in S. cerevisiae. However this one is devoid of transporters belonging to the Manganese Cation Diffusion Facilitator. Eleven transporters belonging to gene families in which Manganese transporters have been found were identified in the P. chrysosporium?s genome. Expression level of these genes was examined particularly in ligninolytic condition. Transporters have also been cloned in order to verify their functions by complementation in heterologous system. This study allowed to identify putative Manganese transporters of numerous fungal organisms and the lack of a transporters family involved in the Manganese transport in S. cerevisia
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Transporteurs fongiques de manganèse : diversité et analyse fonctionnelle chez le champignon saprophyte Panerochaete chrysosporium
HAL CCSD, 2012Co-Authors: Diss LoïcAbstract:P. chrysosporium is a saprophytic fungus able to degrade many xenobiotics which makes it particularly attractive for appliCations in bioremediation. Several publiCations highlight the importance of metal homeostasis in the production of lignolytics enzymes. Indeed the presence of Manganese is required for the production of Manganese peroxidase. Conversely, deficiency allows the production of lignins peroxidases. Characterization of transporters involved in the control of Manganese homeostasis has been only researched in the model S. cerevisiae. Analysis of putative Manganese transporters of 26 fungal species representing 20 orders of fungus was used to form a repertory of 281 transporters of Manganese. Phylogenetic analysis allowed to highlight that dupliCation process, but also deletion, had occurred particularly in S. cerevisiae. However this one is devoid of transporters belonging to the Manganese Cation Diffusion Facilitator. Eleven transporters belonging to gene families in which Manganese transporters have been found were identified in the P. chrysosporium’s genome. Expression level of these genes was examined particularly in ligninolytic condition. Transporters have also been cloned in order to verify their functions by complementation in heterologous system. This study allowed to identify putative Manganese transporters of numerous fungal organisms and the lack of a transporters family involved in the Manganese transport in S. cerevisiae.P. chrysosporium est un champignon saprophyte capable de dégrader de nombreux xénobiotiques, ce qui le rend particulièrement intéressant pour des appliCations en bioremédiation. Plusieurs publiCations mettent en avant l’importance de la maîtrise de l’homéostasie métallique dans la production de certaines enzymes lignolytiques. La présence de manganèse est en effet nécessaire à la production des manganèses peroxydases, alors qu’à l’inverse une carence permettra la production de lignines peroxydases. Cependant, la caractérisation de transporteurs impliqués dans le contrôle de l’homéostasie métallique n’a fait l’objet de recherches poussées que chez le champignon modèle S. cerevisiae. L’analyse des transporteurs putatifs de manganèse de 26 espèces fongiques représentant 20 ordres fongiques a permis de constituer un répertoire de 281 transporteurs de manganèse. L’analyse phylogénétique a permis de mettre en évidence que des processus de dupliCation, mais également de délétion, avaient eu lieu en particulier chez S. cerevisiae. Cependant ce dernier ne posséde pas de transporteurs de manganèse appartenant à la famille des Cation Diffusion Facilitator. Dans le génome de P. chrysosporium, onze transporteurs de manganèse appartenant à différentes familles de gènes ont été identifiés. Le niveau d’expression de ces différents gènes a été étudié notamment en condition lignolytique. Ces transporteurs ont également été clonés afin de vérifier leurs fonctions par complémentation en système hétérologue. Cette étude a permis de mettre en évidence les transporteurs de manganèse putatifs de nombreux organismes fongiques, ainsi que l’absence d’une famille de transporteurs impliquée dans les mouvements de manganèse chez S. cerevisiae
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Transporteurs fongiques de manganèse (diversité et analyse fonctionnelle chez le champignon saprophyte Phanerochaete chrysosporium)
2012Co-Authors: Diss Loïc, Chalot MichelAbstract:P. chrysosporium est un champignon saprophyte capable de dégrader de nombreux xénobiotiques, ce qui le rend particulièrement intéressant pour des appliCations en bioremédiation. Plusieurs publiCations mettent en avant l'importance de la maîtrise de l'homéostasie métallique dans la production de certaines enzymes lignolytiques. La présence de manganèse est en effet nécessaire à la production des manganèses peroxydases, alors qu'à l'inverse une carence permettra la production de lignines peroxydases. Cependant, la caractérisation de transporteurs impliqués dans le contrôle de l'homéostasie métallique n'a fait l'objet de recherches poussées que chez le champignon modèle S. cerevisiae. L'analyse des transporteurs putatifs de manganèse de 26 espèces fongiques représentant 20 ordres fongiques a permis de constituer un répertoire de 281 transporteurs de manganèse. L'analyse phylogénétique a permis de mettre en évidence que des processus de dupliCation, mais également de délétion, avaient eu lieu en particulier chez S. cerevisiae. Cependant ce dernier ne possède pas de transporteurs de manganèse appartenant à la famille des Cation Diffusion Facilitator. Dans le génome de P. chrysosporium, onze transporteurs de manganèse appartenant à différentes familles de gènes ont été identifiés. Le niveau d'expression de ces différents gènes a été étudié notamment en condition lignolytique. Ces transporteurs ont également été clonés afin de vérifier leurs fonctions par complémentation en système hétérologue. Cette étude a permis de mettre en évidence les transporteurs de manganèse putatifs de nombreux organismes fongiques, ainsi que l'absence d'une famille de transporteurs impliquée dans les mouvements de manganèse chez S. cerevisiaeP. chrysosporium is a saprophytic fungus able to degrade many xenobiotics which makes it particularly attractive for appliCations in bioremediation. Several publiCations highlight the importance of metal homeostasis in the production of lignolytics enzymes. Indeed the presence of Manganese is required for the production of Manganese peroxidase. Conversely, deficiency allows the production of lignins peroxidases. Characterization of transporters involved in the control of Manganese homeostasis has been only researched in the model S. cerevisiae. Analysis of putative Manganese transporters of 26 fungal species representing 20 orders of fungus was used to form a repertory of 281 transporters of Manganese. Phylogenetic analysis allowed to highlight that dupliCation process, but also deletion, had occurred particularly in S. cerevisiae. However this one is devoid of transporters belonging to the Manganese Cation Diffusion Facilitator. Eleven transporters belonging to gene families in which Manganese transporters have been found were identified in the P. chrysosporium?s genome. Expression level of these genes was examined particularly in ligninolytic condition. Transporters have also been cloned in order to verify their functions by complementation in heterologous system. This study allowed to identify putative Manganese transporters of numerous fungal organisms and the lack of a transporters family involved in the Manganese transport in S. cerevisiaeMETZ-SCD (574632105) / SudocNANCY1-Bib. numérique (543959902) / SudocNANCY2-Bibliotheque electronique (543959901) / SudocNANCY-INPL-Bib. électronique (545479901) / SudocSudocFranceF
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Transporteurs fongiques de manganèse : diversité et analyse fonctionnelle chez le champignon saprophyte Phanerochaete chrysosporium
HAL CCSD, 2012Co-Authors: Diss LoïcAbstract:P. chrysosporium is a saprophytic fungus able to degrade many xenobiotics which makes it particularly attractive for appliCations in bioremediation. Several publiCations highlight the importance of metal homeostasis in the production of lignolytics enzymes. Indeed the presence of Manganese is required for the production of Manganese peroxidase. Conversely, deficiency allows the production of lignins peroxidases. Characterization of transporters involved in the control of Manganese homeostasis has been only researched in the model S. cerevisiae. Analysis of putative Manganese transporters of 26 fungal species representing 20 orders of fungus was used to form a repertory of 281 transporters of Manganese. Phylogenetic analysis allowed to highlight that dupliCation process, but also deletion, had occurred particularly in S. cerevisiae. However this one is devoid of transporters belonging to the Manganese Cation Diffusion Facilitator. Eleven transporters belonging to gene families in which Manganese transporters have been found were identified in the P. chrysosporium?s genome. Expression level of these genes was examined particularly in ligninolytic condition. Transporters have also been cloned in order to verify their functions by complementation in heterologous system. This study allowed to identify putative Manganese transporters of numerous fungal organisms and the lack of a transporters family involved in the Manganese transport in S. cerevisiaeP. chrysosporium est un champignon saprophyte capable de dégrader de nombreux xénobiotiques, ce qui le rend particulièrement intéressant pour des appliCations en bioremédiation. Plusieurs publiCations mettent en avant l'importance de la maîtrise de l'homéostasie métallique dans la production de certaines enzymes lignolytiques. La présence de manganèse est en effet nécessaire à la production des manganèses peroxydases, alors qu'à l'inverse une carence permettra la production de lignines peroxydases. Cependant, la caractérisation de transporteurs impliqués dans le contrôle de l'homéostasie métallique n'a fait l'objet de recherches poussées que chez le champignon modèle S. cerevisiae. L'analyse des transporteurs putatifs de manganèse de 26 espèces fongiques représentant 20 ordres fongiques a permis de constituer un répertoire de 281 transporteurs de manganèse. L'analyse phylogénétique a permis de mettre en évidence que des processus de dupliCation, mais également de délétion, avaient eu lieu en particulier chez S. cerevisiae. Cependant ce dernier ne possède pas de transporteurs de manganèse appartenant à la famille des Cation Diffusion Facilitator. Dans le génome de P. chrysosporium, onze transporteurs de manganèse appartenant à différentes familles de gènes ont été identifiés. Le niveau d'expression de ces différents gènes a été étudié notamment en condition lignolytique. Ces transporteurs ont également été clonés afin de vérifier leurs fonctions par complémentation en système hétérologue. Cette étude a permis de mettre en évidence les transporteurs de manganèse putatifs de nombreux organismes fongiques, ainsi que l'absence d'une famille de transporteurs impliquée dans les mouvements de manganèse chez S. cerevisia
Anjan Banerjee - One of the best experts on this subject based on the ideXlab platform.
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on the oxidation state of Manganese ions in li ion battery electrolyte solutions
Journal of the American Chemical Society, 2017Co-Authors: Anjan Banerjee, Doron Aurbach, Yuliya Shilina, Baruch Ziv, Joseph M Ziegelbauer, Shalom Luski, Ion C HalalayAbstract:We demonstrate herein that Mn3+ and not Mn2+, as commonly accepted, is the dominant dissolved Manganese Cation in LiPF6-based electrolyte solutions of Li-ion batteries with lithium manganate spinel positive and graphite negative electrodes chemistry. The Mn3+ fractions in solution, derived from a combined analysis of electron paramagnetic resonance and inductively coupled plasma spectroscopy data, are ∼80% for either fully discharged (3.0 V hold) or fully charged (4.2 V hold) cells, and ∼60% for galvanostatically cycled cells. These findings agree with the average oxidation state of dissolved Mn ions determined from X-ray absorption near-edge spectroscopy data, as verified through a speciation diagram analysis. We also show that the fractions of Mn3+ in the aprotic nonaqueous electrolyte solution are constant over the duration of our experiments and that disproportionation of Mn3+ occurs at a very slow rate.
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On the Oxidation State of Manganese Ions in Li-Ion Battery Electrolyte Solutions
2017Co-Authors: Anjan Banerjee, Doron Aurbach, Yuliya Shilina, Baruch Ziv, Joseph M Ziegelbauer, Shalom Luski, Ion C HalalayAbstract:We demonstrate herein that Mn3+ and not Mn2+, as commonly accepted, is the dominant dissolved Manganese Cation in LiPF6-based electrolyte solutions of Li-ion batteries with lithium manganate spinel positive and graphite negative electrodes chemistry. The Mn3+ fractions in solution, derived from a combined analysis of electron paramagnetic resonance and inductively coupled plasma spectroscopy data, are ∼80% for either fully discharged (3.0 V hold) or fully charged (4.2 V hold) cells, and ∼60% for galvanostatically cycled cells. These findings agree with the average oxidation state of dissolved Mn ions determined from X-ray absorption near-edge spectroscopy data, as verified through a speciation diagram analysis. We also show that the fractions of Mn3+ in the aprotic nonaqueous electrolyte solution are constant over the duration of our experiments and that disproportionation of Mn3+ occurs at a very slow rate