Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity ; day:04 ; month:07 ; year:2024 ; extent:11
Angewandte Chemie / International edition. International edition ; (04.07.2024) (gesamt 11)
- Creator
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Kagawa, Yoshiyuki
Oohora, Koji
Himiyama, Tomoki
Suzuki, Akihiro
Hayashi, Takashi
- DOI
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10.1002/anie.202403485
- URN
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urn:nbn:de:101:1-2407081445362.671209167234
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:46 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Kagawa, Yoshiyuki
- Oohora, Koji
- Himiyama, Tomoki
- Suzuki, Akihiro
- Hayashi, Takashi
Other Objects (12)
Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity
Discovery and biosynthesis of the redox cofactor mycofactocin
Nonnatural Reactivity of Cofactor-Dependent Enzymes upon Light Irradiation
Redox Reactivity Control Through Electromerism
carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis
Myoglobin und Myokardinfarkt
Konformationsänderungen in Myoglobin
Targeted redox and energy cofactor metabolomics in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
Metabolic engineering of Escherichia coli for optimized biosynthesis of nicotinamide mononucleotide, a noncanonical redox cofactor
Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies
Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity
Discovery and biosynthesis of the redox cofactor mycofactocin
Nonnatural Reactivity of Cofactor-Dependent Enzymes upon Light Irradiation
Redox Reactivity Control Through Electromerism
carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis
Myoglobin und Myokardinfarkt
Konformationsänderungen in Myoglobin
Targeted redox and energy cofactor metabolomics in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
Metabolic engineering of Escherichia coli for optimized biosynthesis of nicotinamide mononucleotide, a noncanonical redox cofactor
Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies
Redox Engineering of Myoglobin by Cofactor Substitution to Enhance Cyclopropanation Reactivity
Discovery and biosynthesis of the redox cofactor mycofactocin
Nonnatural Reactivity of Cofactor-Dependent Enzymes upon Light Irradiation
Redox Reactivity Control Through Electromerism
carba Nicotinamide Adenine Dinucleotide Phosphate: Robust Cofactor for Redox Biocatalysis
Myoglobin und Myokardinfarkt
Konformationsänderungen in Myoglobin
Targeted redox and energy cofactor metabolomics in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
Human mitochondrial MTHFD2 is a dual redox cofactor-specific methylenetetrahydrofolate dehydrogenase/methenyltetrahydrofolate cyclohydrolase
Redox-dependent substrate-cofactor interactions in the Michaelis-complex of a flavin-dependent oxidoreductase
Metabolic engineering of Escherichia coli for optimized biosynthesis of nicotinamide mononucleotide, a noncanonical redox cofactor