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[NiFe]-hydrogenase maturation
[NiFe]-hydrogenases catalyze the reversible conversion of hydrogen gas into protons and
electrons and are vital metabolic components of many species of bacteria and archaea. At …
electrons and are vital metabolic components of many species of bacteria and archaea. At …
Anaerobic formate and hydrogen metabolism
Numerous recent developments in the biochemistry, molecular biology, and physiology of
formate and H2 metabolism and of the [NiFe]-hydrogenase (Hyd) cofactor biosynthetic …
formate and H2 metabolism and of the [NiFe]-hydrogenase (Hyd) cofactor biosynthetic …
Moving nickel along the hydrogenase–urease maturation pathway
Hydrogenases and ureases play vital metabolic functions in all three domains of life.
However, nickel ions are cytotoxic because they can inactivate enzymes that require less …
However, nickel ions are cytotoxic because they can inactivate enzymes that require less …
A novel mode of control of nickel uptake by a multifunctional metallochaperone
Cellular metal homeostasis is a critical process for all organisms, requiring tight regulation.
In the major pathogen Helicobacter pylori, the acquisition of nickel is an essential virulence …
In the major pathogen Helicobacter pylori, the acquisition of nickel is an essential virulence …
High-Yield Production of Catalytically Active Regulatory [NiFe]-Hydrogenase From Cupriavidus necator in Escherichia coli
Hydrogenases are biotechnologically relevant metalloenzymes that catalyze the reversible
conversion of molecular hydrogen into protons and electrons. The O2-tolerant [NiFe] …
conversion of molecular hydrogen into protons and electrons. The O2-tolerant [NiFe] …
Enhancement of Escherichia coli bacterial biomass and hydrogen production by some heavy metal ions and their mixtures during glycerol vs glucose fermentation at a …
Escherichia coli growth and H 2 production were followed in the presence of heavy metal
ions and their mixtures during glycerol or glucose fermentation at pH 5.5–7.5. Ni 2+(50 μM) …
ions and their mixtures during glycerol or glucose fermentation at pH 5.5–7.5. Ni 2+(50 μM) …
Positive charges promote the recognition of proteins by the chaperone SlyD from Escherichia coli
D Lindemeier, W Graubner, D Mehner-Breitfeld… - Plos one, 2024 - journals.plos.org
SlyD is a widely-occurring prokaryotic FKBP-family prolyl isomerase with an additional
chaperone domain. Often, such as in Escherichia coli, a third domain is found at its C …
chaperone domain. Often, such as in Escherichia coli, a third domain is found at its C …
A whole-cell, high-throughput hydrogenase assay to identify factors that modulate [NiFe]-hydrogenase activity
[NiFe]-hydrogenases have attracted attention as potential therapeutic targets or components
of a hydrogen-based economy.[NiFe]-hydrogenase production is a complicated process that …
of a hydrogen-based economy.[NiFe]-hydrogenase production is a complicated process that …
Exploration into the nickel 'microcosmos' in prokaryotes
Nickel participates in important biochemical processes in many prokaryotes. Nickel-
requiring microorganisms thus have developed elaborate systems to maintain the …
requiring microorganisms thus have developed elaborate systems to maintain the …
Nickel metalloregulators and chaperones
K Higgins - Inorganics, 2019 - mdpi.com
Nickel is essential for the survival of many pathogenic bacteria. E. coli and H. pylori require
nickel for [NiFe]-hydrogenases. H. pylori also requires nickel for urease. At high …
nickel for [NiFe]-hydrogenases. H. pylori also requires nickel for urease. At high …