Transition Metals in Catalysis: The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems

Bibliographic Details
Title: Transition Metals in Catalysis: The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems
Authors: Silke Leimkühler
Source: Inorganics, Vol 9, Iss 1, p 6 (2021)
Publisher Information: MDPI AG, 2021.
Publication Year: 2021
Collection: LCC:Inorganic chemistry
Subject Terms: n/a, Inorganic chemistry, QD146-197
More Details: Following the “Molybdenum and Tungsten Enzyme conference—MoTEC2019” and the satellite meeting on “Iron–Sulfur for Life”, we wanted to emphasize the link between iron–sulfur clusters and their importance for the biosynthesis, assembly, and activity of complex metalloenzymes in this Special Issue of Inorganics, entitled “Transition Metals in Catalysis: The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems” [...]
Document Type: article
File Description: electronic resource
Language: English
ISSN: 2304-6740
Relation: https://www.mdpi.com/2304-6740/9/1/6; https://doaj.org/toc/2304-6740
DOI: 10.3390/inorganics9010006
Access URL: https://doaj.org/article/3604cb89a5fb4b468edd50daaf83e184
Accession Number: edsdoj.3604cb89a5fb4b468edd50daaf83e184
Database: Directory of Open Access Journals
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  Data: Transition Metals in Catalysis: The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems
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  Data: Inorganics, Vol 9, Iss 1, p 6 (2021)
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  Data: MDPI AG, 2021.
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  Data: Following the “Molybdenum and Tungsten Enzyme conference—MoTEC2019” and the satellite meeting on “Iron–Sulfur for Life”, we wanted to emphasize the link between iron–sulfur clusters and their importance for the biosynthesis, assembly, and activity of complex metalloenzymes in this Special Issue of Inorganics, entitled “Transition Metals in Catalysis: The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems” [...]
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