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  • 1
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    A radical intermediate in tyrosine scission to the CO and CN- ligands of FeFe hydrogenase (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-10-26
    Description: The radical S-adenosylmethionine (SAM) enzyme HydG lyses free l-tyrosine to produce CO and CN(-) for the assembly of the catalytic H cluster of FeFe hydrogenase. We used electron paramagnetic resonance spectroscopy to detect and characterize HydG reaction intermediates generated with a set of (2)H, (13)C, and (15)N nuclear spin-labeled tyrosine substrates. We propose a detailed reaction mechanism in which the radical SAM reaction, initiated at an N-terminal 4Fe-4S cluster, generates a tyrosine radical bound to a C-terminal 4Fe-4S cluster. Heterolytic cleavage of this tyrosine radical at the Calpha-Cbeta bond forms a transient 4-oxidobenzyl (4OB(*)) radical and a dehydroglycine bound to the C-terminal 4Fe-4S cluster. Electron and proton transfer to this 4OB(*) radical forms p-cresol, with the conversion of this dehydroglycine ligand to Fe-bound CO and CN(-), a key intermediate in the assembly of the 2Fe subunit of the H cluster.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuchenreuther, Jon M -- Myers, William K -- Stich, Troy A -- George, Simon J -- Nejatyjahromy, Yaser -- Swartz, James R -- Britt, R David -- R01 GM104543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2013 Oct 25;342(6157):472-5. doi: 10.1126/science.1241859.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Davis, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24159045" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/genetics ; Carbon Monoxide/chemistry ; Catalysis ; Catalytic Domain ; Hydrogenase/*chemistry ; Iron-Sulfur Proteins/*chemistry/genetics ; Ligands ; S-Adenosylmethionine/chemistry ; Shewanella/*enzymology ; Tyrosine/*chemistry
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster (2014)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2014-01-25
    Description: Three iron-sulfur proteins--HydE, HydF, and HydG--play a key role in the synthesis of the [2Fe](H) component of the catalytic H-cluster of FeFe hydrogenase. The radical S-adenosyl-L-methionine enzyme HydG lyses free tyrosine to produce p-cresol and the CO and CN(-) ligands of the [2Fe](H) cluster. Here, we applied stopped-flow Fourier transform infrared and electron-nuclear double resonance spectroscopies to probe the formation of HydG-bound Fe-containing species bearing CO and CN(-) ligands with spectroscopic signatures that evolve on the 1- to 1000-second time scale. Through study of the (13)C, (15)N, and (57)Fe isotopologs of these intermediates and products, we identify the final HydG-bound species as an organometallic Fe(CO)2(CN) synthon that is ultimately transferred to apohydrogenase to form the [2Fe](H) component of the H-cluster.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4514031/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4514031/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuchenreuther, Jon M -- Myers, William K -- Suess, Daniel L M -- Stich, Troy A -- Pelmenschikov, Vladimir -- Shiigi, Stacey A -- Cramer, Stephen P -- Swartz, James R -- Britt, R David -- George, Simon J -- GM072623/GM/NIGMS NIH HHS/ -- GM65440/GM/NIGMS NIH HHS/ -- R01 GM065440/GM/NIGMS NIH HHS/ -- R01 GM104543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2014 Jan 24;343(6169):424-7. doi: 10.1126/science.1246572.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Davis, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24458644" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry ; Catalysis ; *Catalytic Domain ; Hydrogenase/*chemistry ; Iron Carbonyl Compounds/*metabolism ; Iron-Sulfur Proteins/*chemistry ; Shewanella putrefaciens/enzymology ; Spectroscopy, Fourier Transform Infrared
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Role for cysteine in FeFe hydrogenase maturation [Biochemistry] (2015)
    National Academy of Sciences
    Details
    Publication Date: 2015-09-16
    Description: Hydrogenases catalyze the redox interconversion of protons and H2, an important reaction for a number of metabolic processes and for solar fuel production. In FeFe hydrogenases, catalysis occurs at the H cluster, a metallocofactor comprising a [4Fe–4S]H subcluster coupled to a [2Fe]H subcluster bound by CO, CN–, and azadithiolate ligands....
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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