The cyanide ligands of [FeFe] hydrogenase: pulse EPR studies of (13)C and (15)N-labeled H-cluster.
The two cyanide ligands in the assembled cluster of [FeFe] hydrogenase originate from exogenous l-tyrosine. Using selectively labeled tyrosine substrates, the cyanides were isotopically labeled via a recently developed in vitro maturation procedure allowing advanced electron paramagnetic resonance t...
Hlavní autoři: | Myers, W, Stich, T, Suess, D, Kuchenreuther, J, Swartz, JR, Britt, R |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
American Chemical Society
2014
|
Podobné jednotky
-
A radical intermediate in tyrosine scission to the CO and CN⁻ ligands of FeFe hydrogenase
Autor: Kuchenreuther, J, a další
Vydáno: (2013) -
New insights into [FeFe] hydrogenase activation and maturase function.
Autor: Jon M Kuchenreuther, a další
Vydáno: (2012-01-01) -
The HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster.
Autor: Kuchenreuther, J, a další
Vydáno: (2014) -
Tyrosine, cysteine, and S-adenosyl methionine stimulate in vitro [FeFe] hydrogenase activation.
Autor: Jon M Kuchenreuther, a další
Vydáno: (2009-10-01) -
High-yield expression of heterologous [FeFe] hydrogenases in Escherichia coli.
Autor: Jon M Kuchenreuther, a další
Vydáno: (2010-01-01)