The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster.
Three iron-sulfur proteins–HydE, HydF, and HydG–play a key role in the synthesis of the [2Fe]<sub>H</sub> component of the catalytic H-cluster of FeFe hydrogenase. The radical <em>S</em>-adenosyl-<span style="font-variant: small-caps;">l</span>-methionin...
المؤلفون الرئيسيون: | Kuchenreuther, J, Myers, W, Suess, D, Stich, T, Pelmenschikov, V, Shiigi, SA, Cramer, S, Swartz, JR, Britt, R, George, S |
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التنسيق: | Journal article |
اللغة: | English |
منشور في: |
American Association for the Advancement of Science
2014
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مواد مشابهة
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Proposed Mechanism for the Biosynthesis of the [FeFe] Hydrogenase H‑Cluster: Central Roles for the Radical SAM Enzymes HydG and HydE
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A radical intermediate in tyrosine scission to the CO and CN⁻ ligands of FeFe hydrogenase
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The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster.
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New insights into [FeFe] hydrogenase activation and maturase function.
حسب: Jon M Kuchenreuther, وآخرون
منشور في: (2012-01-01) -
Unraveling the H-cluster biosynthetic pathway: Investigations of radical SAM chemistry catalyzed by the HydG maturase
حسب: Kuchenreuther, J, وآخرون
منشور في: (2013)