FEBS Letters | |
Characterization of the active site of a hydrogen sensor from Alcaligenes eutrophus | |
Lenz, Oliver2  Albracht, Simon P.J1  Friedrich, Bärbel2  Pierik, Antonio J1  Schmelz, Milena2  | |
[1]E.C. Slater Institute, Biochemistry, University of Amsterdam, Plantage Muidergracht 12, NL-1018 TV Amsterdam, The Netherlands | |
[2]Institut für Biologie/Mikrobiologie, Humboldt-Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany | |
关键词: Hydrogen; Sensor; Active site; Hydrogenase; Electron paramagnetic resonance; Fourier transform infrared spectroscopy; SH; soluble (cytoplasmic) hydrogenase; MBH; membrane-bound hydrogenase; RH; regulatory hydrogenase from A. eutrophus; RH+; cells deficient in both the SH and the MBH; in which the RH was overproduced from the vector pGE378; RH−; cells deficient in both the SH and the MBH; containing the vector control pEDY309; | |
DOI : 10.1016/S0014-5793(98)01306-4 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
A third hydrogenase was recently identified in the proteobacterium Alcaligenes eutrophus as a constituent of a novel H2-sensing multicomponent regulatory system. This regulatory hydrogenase (RH) has been overexpressed in cells deficient in both the NAD+-reducing [NiFe]-hydrogenase and the membrane-bound [NiFe]-hydrogenase. EPR, FTIR and activity studies of membrane-free extracts revealed that the RH has an active site much like that of standard [NiFe]-hydrogenases, i.e. a Ni-Fe site with two CN− groups and one CO molecule. Its catalytic power is low, but the RH is always active, insensitive to oxygen, and occurs in only two redox states.
【 授权许可】
Unknown
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