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
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