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Taming of a Poison: Biosynthesis of the NiFe-Hydrogenase Cyanide Ligands.

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Title: Taming of a Poison: Biosynthesis of the NiFe-Hydrogenase Cyanide Ligands.
Authors: Reissmann, Stefanie, Hochleitner, Elisabeth, Wang, Haofan, Paschos, Athanasios, Lottspeich, Friedrich, Glass, Richard S., Böck, August
Source: Science (pre-March 2025). 2/14/2003, Vol. 299 Issue 5609, p1067-1070. 4p. 2 Diagrams, 2 Graphs.
Subjects: Cyanides, Biosynthesis
Abstract: NiFe-hydrogenases have an Ni-Fe site in which the iron has one CO and two CN groups as ligands. Synthesis of the CN ligands requires the activity of two hydrogenase maturation proteins: HypF and HypE. HypF is a carbamoyltransferase that transfers the carbamoyl moiety of carbamoyladenylate to the COOH-terminal cysteine of HypE and thus forms an enzyme-thiocarbamate. HypE dehydrates the S-carbamoyl moiety in an adenosine triphosphate—dependent process to yield the enzyme thiocyanate. Chemical model reactions corroborate the feasibility of this unprecedented biosynthetic route and show that thiocyanates can donate CN to iron. This finding underscores a striking parallel between biochemistry and organometallic chemistry in the formation of an iron-cyano complex. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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  Data: Taming of a Poison: Biosynthesis of the NiFe-Hydrogenase Cyanide Ligands.
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  Data: <searchLink fieldCode="AR" term="%22Reissmann%2C+Stefanie%22">Reissmann, Stefanie</searchLink><br /><searchLink fieldCode="AR" term="%22Hochleitner%2C+Elisabeth%22">Hochleitner, Elisabeth</searchLink><br /><searchLink fieldCode="AR" term="%22Wang%2C+Haofan%22">Wang, Haofan</searchLink><br /><searchLink fieldCode="AR" term="%22Paschos%2C+Athanasios%22">Paschos, Athanasios</searchLink><br /><searchLink fieldCode="AR" term="%22Lottspeich%2C+Friedrich%22">Lottspeich, Friedrich</searchLink><br /><searchLink fieldCode="AR" term="%22Glass%2C+Richard+S%2E%22">Glass, Richard S.</searchLink><br /><searchLink fieldCode="AR" term="%22Böck%2C+August%22">Böck, August</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 2/14/2003, Vol. 299 Issue 5609, p1067-1070. 4p. 2 Diagrams, 2 Graphs.
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  Data: <searchLink fieldCode="DE" term="%22Cyanides%22">Cyanides</searchLink><br /><searchLink fieldCode="DE" term="%22Biosynthesis%22">Biosynthesis</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: NiFe-hydrogenases have an Ni-Fe site in which the iron has one CO and two CN groups as ligands. Synthesis of the CN ligands requires the activity of two hydrogenase maturation proteins: HypF and HypE. HypF is a carbamoyltransferase that transfers the carbamoyl moiety of carbamoyladenylate to the COOH-terminal cysteine of HypE and thus forms an enzyme-thiocarbamate. HypE dehydrates the S-carbamoyl moiety in an adenosine triphosphate—dependent process to yield the enzyme thiocyanate. Chemical model reactions corroborate the feasibility of this unprecedented biosynthetic route and show that thiocyanates can donate CN to iron. This finding underscores a striking parallel between biochemistry and organometallic chemistry in the formation of an iron-cyano complex. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
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  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1126/science.1080972
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        Text: English
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              Text: 2/14/2003
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              Y: 2003
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