Journal
SCIENCE
Volume 343, Issue 6169, Pages 424-427Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1246572
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Funding
- NIH [GM072623, GM65440]
- Division of Material Sciences and Engineering of the Office of Basic Energy Sciences of the U.S. Department of Energy (DOE) [DE-FG02-09ER46632]
- Office of Biological and Environmental Research of the DOE
- UniCat Cluster of Excellence of the German Research Council
- Engineering and Physical Sciences Research Council [EP/D048559/1, EP/L011972/1] Funding Source: researchfish
- EPSRC [EP/D048559/1, EP/L011972/1] Funding Source: UKRI
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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 C-13, N-15, and Fe-57 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.
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