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Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha
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| Zeitschriftentitel: | FEBS Letters |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | FEBS Letters, 581, 2007, 17, S. 3322-3326 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Lenz, Oliver Zebger, Ingo Hamann, Josta Hildebrandt, Peter Friedrich, Bärbel Lenz, Oliver Zebger, Ingo Hamann, Josta Hildebrandt, Peter Friedrich, Bärbel |
|---|---|
| author |
Lenz, Oliver Zebger, Ingo Hamann, Josta Hildebrandt, Peter Friedrich, Bärbel |
| spellingShingle |
Lenz, Oliver Zebger, Ingo Hamann, Josta Hildebrandt, Peter Friedrich, Bärbel FEBS Letters Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| author_sort |
lenz, oliver |
| spelling |
Lenz, Oliver Zebger, Ingo Hamann, Josta Hildebrandt, Peter Friedrich, Bärbel 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2007.06.027 <jats:p>Within the catalytic centre of [NiFe]‐hydrogenases one carbonyl and two cyanide ligands are covalently attached to the iron. To identify the metabolic origins of these ligands, the regulatory [NiFe] hydrogenase in conjunction with the indigenous Hyp maturation proteins of <jats:italic>Ralstonia eutropha</jats:italic> H16 were heterologously overproduced in <jats:italic>E. coli</jats:italic> grown in the presence of <jats:sc>l</jats:sc>‐[ureido‐<jats:sup>13</jats:sup>C] citrulline and NaH<jats:sup>13</jats:sup>CO<jats:sub>3</jats:sub>. Infrared spectroscopy of purified hydrogenase provided direct evidence that only the cyanide ligands, but not the CO ligand, originate from CO<jats:sub>2</jats:sub> and carbamoylphosphate. Incorporation of label from <jats:sup>13</jats:sup>CO exclusively into the carbonyl ligand indicates that free CO is a possible precursor in carbonyl ligand biosynthesis.</jats:p> Carbamoylphosphate serves as the source of CN<sup>−</sup>, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from <i>Ralstonia eutropha</i> FEBS Letters |
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10.1016/j.febslet.2007.06.027 |
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| title |
Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_unstemmed |
Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_full |
Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_fullStr |
Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_full_unstemmed |
Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_short |
Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_sort |
carbamoylphosphate serves as the source of cn<sup>−</sup>, but not of the intrinsic co in the active site of the regulatory [nife]‐hydrogenase from <i>ralstonia eutropha</i> |
| topic |
Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics |
| url |
http://dx.doi.org/10.1016/j.febslet.2007.06.027 |
| publishDate |
2007 |
| physical |
3322-3326 |
| description |
<jats:p>Within the catalytic centre of [NiFe]‐hydrogenases one carbonyl and two cyanide ligands are covalently attached to the iron. To identify the metabolic origins of these ligands, the regulatory [NiFe] hydrogenase in conjunction with the indigenous Hyp maturation proteins of <jats:italic>Ralstonia eutropha</jats:italic> H16 were heterologously overproduced in <jats:italic>E. coli</jats:italic> grown in the presence of <jats:sc>l</jats:sc>‐[ureido‐<jats:sup>13</jats:sup>C] citrulline and NaH<jats:sup>13</jats:sup>CO<jats:sub>3</jats:sub>. Infrared spectroscopy of purified hydrogenase provided direct evidence that only the cyanide ligands, but not the CO ligand, originate from CO<jats:sub>2</jats:sub> and carbamoylphosphate. Incorporation of label from <jats:sup>13</jats:sup>CO exclusively into the carbonyl ligand indicates that free CO is a possible precursor in carbonyl ligand biosynthesis.</jats:p> |
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| description | <jats:p>Within the catalytic centre of [NiFe]‐hydrogenases one carbonyl and two cyanide ligands are covalently attached to the iron. To identify the metabolic origins of these ligands, the regulatory [NiFe] hydrogenase in conjunction with the indigenous Hyp maturation proteins of <jats:italic>Ralstonia eutropha</jats:italic> H16 were heterologously overproduced in <jats:italic>E. coli</jats:italic> grown in the presence of <jats:sc>l</jats:sc>‐[ureido‐<jats:sup>13</jats:sup>C] citrulline and NaH<jats:sup>13</jats:sup>CO<jats:sub>3</jats:sub>. Infrared spectroscopy of purified hydrogenase provided direct evidence that only the cyanide ligands, but not the CO ligand, originate from CO<jats:sub>2</jats:sub> and carbamoylphosphate. Incorporation of label from <jats:sup>13</jats:sup>CO exclusively into the carbonyl ligand indicates that free CO is a possible precursor in carbonyl ligand biosynthesis.</jats:p> |
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| spelling | Lenz, Oliver Zebger, Ingo Hamann, Josta Hildebrandt, Peter Friedrich, Bärbel 0014-5793 1873-3468 Wiley Cell Biology Genetics Molecular Biology Biochemistry Structural Biology Biophysics http://dx.doi.org/10.1016/j.febslet.2007.06.027 <jats:p>Within the catalytic centre of [NiFe]‐hydrogenases one carbonyl and two cyanide ligands are covalently attached to the iron. To identify the metabolic origins of these ligands, the regulatory [NiFe] hydrogenase in conjunction with the indigenous Hyp maturation proteins of <jats:italic>Ralstonia eutropha</jats:italic> H16 were heterologously overproduced in <jats:italic>E. coli</jats:italic> grown in the presence of <jats:sc>l</jats:sc>‐[ureido‐<jats:sup>13</jats:sup>C] citrulline and NaH<jats:sup>13</jats:sup>CO<jats:sub>3</jats:sub>. Infrared spectroscopy of purified hydrogenase provided direct evidence that only the cyanide ligands, but not the CO ligand, originate from CO<jats:sub>2</jats:sub> and carbamoylphosphate. Incorporation of label from <jats:sup>13</jats:sup>CO exclusively into the carbonyl ligand indicates that free CO is a possible precursor in carbonyl ligand biosynthesis.</jats:p> Carbamoylphosphate serves as the source of CN<sup>−</sup>, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from <i>Ralstonia eutropha</i> FEBS Letters |
| spellingShingle | Lenz, Oliver, Zebger, Ingo, Hamann, Josta, Hildebrandt, Peter, Friedrich, Bärbel, FEBS Letters, Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha, Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| title | Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_full | Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_fullStr | Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_full_unstemmed | Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_short | Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| title_sort | carbamoylphosphate serves as the source of cn<sup>−</sup>, but not of the intrinsic co in the active site of the regulatory [nife]‐hydrogenase from <i>ralstonia eutropha</i> |
| title_unstemmed | Carbamoylphosphate serves as the source of CN−, but not of the intrinsic CO in the active site of the regulatory [NiFe]‐hydrogenase from Ralstonia eutropha |
| topic | Cell Biology, Genetics, Molecular Biology, Biochemistry, Structural Biology, Biophysics |
| url | http://dx.doi.org/10.1016/j.febslet.2007.06.027 |