Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site ; year:2021
Angewandte Chemie ; (2021)
- Creator
- DOI
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10.1002/ange.202015751
- URN
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urn:nbn:de:101:1-2021020410505064827164
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:20 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
- Buscagan, Trixia M.
- Perez, Kathryn A.
- Maggiolo, Ailiena O.
- Rees, Douglas C.
- Spatzal, Thomas
Other Objects (12)
Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site
Electronic Structure Studies of Iron-Sulfur Clusters: from Model Compounds to the Active Site of Nitrogenase
Fe protein docking transduces conformational changes to MoFe nitrogenase active site in a nucleotide-dependent manner
Critical evaluation of a crystal structure of nitrogenase with bound N2 ligands
Specificity of NifEN and VnfEN for the assembly of nitrogenase active site cofactors in Azotobacter vinelandii
Additional Remarks on Active Molecules
Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase
Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase
Active particles bound by information flows
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle
para ‐Aminoazobenzenes—Bipolar Redox‐Active Molecules
Active colloidal molecules in activity gradients
Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site
Electronic Structure Studies of Iron-Sulfur Clusters: from Model Compounds to the Active Site of Nitrogenase
Fe protein docking transduces conformational changes to MoFe nitrogenase active site in a nucleotide-dependent manner
Critical evaluation of a crystal structure of nitrogenase with bound N2 ligands
Specificity of NifEN and VnfEN for the assembly of nitrogenase active site cofactors in Azotobacter vinelandii
Additional Remarks on Active Molecules
Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase
Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase
Active particles bound by information flows
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle
para ‐Aminoazobenzenes—Bipolar Redox‐Active Molecules
Active colloidal molecules in activity gradients
Structural Characterization of Two CO Molecules Bound to the Nitrogenase Active Site
Electronic Structure Studies of Iron-Sulfur Clusters: from Model Compounds to the Active Site of Nitrogenase
Fe protein docking transduces conformational changes to MoFe nitrogenase active site in a nucleotide-dependent manner
Critical evaluation of a crystal structure of nitrogenase with bound N2 ligands
Specificity of NifEN and VnfEN for the assembly of nitrogenase active site cofactors in Azotobacter vinelandii
Additional Remarks on Active Molecules
Chimeric Interaction of Nitrogenase‐Like Reductases with the MoFe Protein of Nitrogenase
Chimeric interaction of nitrogenase‐like reductases with the MoFe protein of nitrogenase
Active particles bound by information flows
Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle
para ‐Aminoazobenzenes—Bipolar Redox‐Active Molecules