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Characterization of the active site of a hydrogen sensor from Alcaligenes eutrophus
Author(s) -
Pierik Antonio J,
Schmelz Milena,
Lenz Oliver,
Friedrich Bärbel,
Albracht Simon P.J
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01306-4
Subject(s) - alcaligenes , chemistry , characterization (materials science) , biochemistry , active site , biology , bacteria , catalysis , materials science , nanotechnology , genetics , pseudomonas
A third hydrogenase was recently identified in the proteobacterium Alcaligenes eutrophus as a constituent of a novel H 2 ‐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.