AbstractAssembly of the active site of the [NiFe]-hydrogenase enzymes involves a multi-step pathway and the coordinated activity of many accessory proteins. To analyze complex formation between these factors in Escherichia coli, they were genomically tagged and native multi-protein complexes were isolated. This method validated multiple interactions reported in separate studies from several organisms and defined a new complex containing the putative chaperone HybG and the large subunit of hydrogenase 1 or 2. The complex also includes HypE and HypD, which interact with each other before joining the larger complex
[NiFe]-hydrogenases catalyze the reversible oxidation of hydrogen gas at a bimetallic active site an...
Nickel insertion into the [NiFe]-hydrogenase requires the accessory protein HypB, which is a GTPase....
[NiFe]-hydrogenases catalyze the reversible conversion of hydrogen gas into protons and electrons an...
AbstractAssembly of the active site of the [NiFe]-hydrogenase enzymes involves a multi-step pathway ...
AbstractThe multi-step biosynthesis of the [NiFe]-hydrogenase enzyme involves a variety of accessory...
[NiFe] hydrogenases are found in a variety of microorganisms and catalyze the reversible oxidation o...
[NiFe]-hydrogenases (Hyd) bind a nickel-iron-based cofactor. The Fe ion of the cofactor is bound by...
Summary[NiFe]-hydrogenases are multimeric proteins. The large subunit contains the NiFe(CN)2CO bimet...
The active site of [NiFe]-hydrogenase contains nickel and iron coordinated by cysteine residues, cya...
<div><p>The active site of [NiFe]-hydrogenase contains nickel and iron coordinated by cysteine resid...
[NiFe]-hydrogenase enzymes catalyze the reversible reduction of protons to molecular hydrogen and se...
The hybG gene product from Escherichia coli has been identified as a chaperone-like protein acting i...
The maturation of [NiFe]-hydrogenase in <i>Escherichia coli</i> is a complex process involving many ...
The assembly of multi-protein complexes requires the concerted synthesis and maturation of its compo...
Salmonella enterica serovar Typhimurium has the ability to use molecular hydrogen as a respiratory e...
[NiFe]-hydrogenases catalyze the reversible oxidation of hydrogen gas at a bimetallic active site an...
Nickel insertion into the [NiFe]-hydrogenase requires the accessory protein HypB, which is a GTPase....
[NiFe]-hydrogenases catalyze the reversible conversion of hydrogen gas into protons and electrons an...
AbstractAssembly of the active site of the [NiFe]-hydrogenase enzymes involves a multi-step pathway ...
AbstractThe multi-step biosynthesis of the [NiFe]-hydrogenase enzyme involves a variety of accessory...
[NiFe] hydrogenases are found in a variety of microorganisms and catalyze the reversible oxidation o...
[NiFe]-hydrogenases (Hyd) bind a nickel-iron-based cofactor. The Fe ion of the cofactor is bound by...
Summary[NiFe]-hydrogenases are multimeric proteins. The large subunit contains the NiFe(CN)2CO bimet...
The active site of [NiFe]-hydrogenase contains nickel and iron coordinated by cysteine residues, cya...
<div><p>The active site of [NiFe]-hydrogenase contains nickel and iron coordinated by cysteine resid...
[NiFe]-hydrogenase enzymes catalyze the reversible reduction of protons to molecular hydrogen and se...
The hybG gene product from Escherichia coli has been identified as a chaperone-like protein acting i...
The maturation of [NiFe]-hydrogenase in <i>Escherichia coli</i> is a complex process involving many ...
The assembly of multi-protein complexes requires the concerted synthesis and maturation of its compo...
Salmonella enterica serovar Typhimurium has the ability to use molecular hydrogen as a respiratory e...
[NiFe]-hydrogenases catalyze the reversible oxidation of hydrogen gas at a bimetallic active site an...
Nickel insertion into the [NiFe]-hydrogenase requires the accessory protein HypB, which is a GTPase....
[NiFe]-hydrogenases catalyze the reversible conversion of hydrogen gas into protons and electrons an...