The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the [Fe]‐Hydrogenase Cofactor-Reference-Cited by-同舟云学术

The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the [Fe]‐Hydrogenase Cofactor

Published:2022-11-17 Issue:50 Volume:134 Page:
ISSN:0044-8249
Container-title:Angewandte Chemie
language:en
Short-container-title:Angewandte Chemie

Author:

Arriaza‐Gallardo Francisco J.¹,Schaupp Sebastian¹,Zheng Yu‐Cong¹,Abdul‐Halim Mohd Farid²,Pan Hui‐Jie³,Kahnt Jörg¹,Angelidou Georgia¹,Paczia Nicole¹,Hu Xile³,Costa Kyle²,Shima Seigo¹^ORCID

Affiliation:

1. Max Planck Institute for Terrestrial Microbiology Karl-von-Frisch-Straße 10 35043 Marburg Germany

2. Department of Plant and Microbial Biology University of Minnesota Twin Cities, St. Paul Minnesota USA

3. Laboratory of Inorganic Synthesis and Catalysis Institute of Chemical Sciences and Engineering Ecole Polytechnique Fédérale de Lausanne (EPFL) ISIC-LSCI, BCH 3305 Lausanne 1015 Switzerland

Funder

Deutsche Forschungsgemeinschaft

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

U.S. Department of Energy

International Max Planck Research School for Environmental, Cellular and Molecular Microbiology

Max-Planck-Gesellschaft

Publisher

Wiley

Subject

General Medicine

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/ange.202213239

Reference39 articles.

2. The crystal structure of C176A mutated [Fe]‐hydrogenase suggests an acyl‐iron ligation in the active site iron complex

3. The Crystal Structure of [Fe]-Hydrogenase Reveals the Geometry of the Active Site

4. The Cofactor of the Iron–Sulfur Cluster Free Hydrogenase Hmd: Structure of the Light-Inactivation Product

5. The Cofactor of the Iron–Sulfur Cluster Free Hydrogenase Hmd: Structure of the Light-Inactivation Product