A membrane‐bound [NiFe]‐hydrogenase large subunit precursor whose C‐terminal extension is not essential for cofactor incorporation but guarantees optimal maturation
Author:
Affiliation:
1. Institut für Chemie Physikalische Chemie Technische Universität Berlin Berlin Germany
Funder
Einstein Stiftung Berlin
Publisher
Wiley
Subject
Microbiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/mbo3.1029
Reference49 articles.
1. Identification of a stable complex between a [NiFe]-hydrogenase catalytic subunit and its maturation protease
2. Computational analyses, molecular dynamics, and mutagenesis studies of unprocessed form of [NiFe] hydrogenase reveal the role of disorder for efficient enzyme maturation
3. Infrared-Detectable Group Senses Changes in Charge Density on the Nickel Center in Hydrogenase from Chromatium vinosum
4. The H2 Sensor of Ralstonia eutropha
5. The Alcaligenes eutrophus membrane-bound hydrogenase gene locus encodes functions involved in maturation and electron transport coupling
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1. Stepwise assembly of the active site of [NiFe]-hydrogenase;Nature Chemical Biology;2023-01-26
2. Conformational and mechanical stability of the isolated large subunit of membrane-bound [NiFe]-hydrogenase from Cupriavidus necator;Frontiers in Microbiology;2023-01-17
3. High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase From Cupriavidus necator in Escherichia coli;Frontiers in Microbiology;2022-04-29
4. In Vivo Assembly of a Genetically Encoded Artificial Metalloenzyme for Hydrogen Production;ACS Synthetic Biology;2021-08-09
5. Optimization of Culture Conditions for Oxygen-Tolerant Regulatory [NiFe]-Hydrogenase Production from Ralstonia eutropha H16 in Escherichia coli;Microorganisms;2021-05-31
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