Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 13, Issue 8, Pages 1315-1320Publisher
SPRINGER
DOI: 10.1007/s00775-008-0412-5
Keywords
Hydrogenase; Infrared; Selenocysteine; Spectroelectrochemistry
Funding
- Ministerio de Educacion y Ciencia [CTQ2006-12097,]
- Fundacao para a Ciencia e Tecnologia FCT, MCES, Portugal [PTDC/BIA-PRO/70429/2006]
- FEDER
- Conselho de Reitores das Universidades Portuguesas Portugal
- Ministerio de Educacio n y Ciencia Spain
- Fundação para a Ciência e a Tecnologia [PTDC/BIA-PRO/70429/2006] Funding Source: FCT
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For the first time a complete characterization by infrared spectroscopy of a Ni-Fe-Se hydrogenase in its different redox states is reported. The Ni-Fe-Se hydrogenase was isolated from Desulfovibrio vulgaris Hildenborough. Two different electron paramagnetic resonance silent and air-stable redox states that are not in equilibrium were detected. Upon reduction of these states the catalytically active states Ni-R and Ni-C appear immediately. These states are in redox equilibrium and their formal redox potential has been measured. Putative structural differences between the redox states of the active site of the Ni-Fe-Se hydrogenase are discussed.
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