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J Biol Chem, Vol. 273, Issue 16, 10019-10025, April 17, 1998
From the Department of Biochemistry, University of Wisconsin,
Madison, Wisconsin 53706
CooJ, a nickel-binding protein from the CO
dehydrogenase system of Rhodospirillum rubrum, was purified
by immobilized metal affinity chromatography. CooJ is a CO-induced
protein predicted to contain a nickel binding motif composed of 16 histidine residues in the final 34 amino acids of the 12.5-kDa protein.
When cells grown in the presence of CO were fractionated on an
immobilized metal affinity chromatography column and analyzed by
SDS-polyacrylamide gel electrophoresis, the major protein observed in
the effluent migrated at an apparent molecular mass of 19 kDa. The
19-kDa protein was absent in extracts of cells grown in the absence of
CO and the mutant strain, UR294, which lacks a functional
cooJ gene. N-terminal sequence analysis confirmed that the
19-kDa protein is the product of the cooJ gene. Purified
CooJ was shown to bind four nickel atoms per CooJ monomer with a
Kd of 4.3 µM. Other divalent metals
competed with the following order of affinity and corresponding
Ki: Zn2+ (5 µM) > Cd2+ (19 µM) > Co2+ (23 µM) > Cu2+ (122 µM). CooJ
chromatographed on a calibrated Superose 12 gel filtration column
eluted at 39 kDa, a position consistent with a multimeric native
molecular mass for CooJ.
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