Abstract.
In Methanococcus voltae, one of the two [NiFeSe] hydrogenases is unusual in that the large subunit is split into two subunits, each contributing two ligands to the [NiFe] center that catalyzes the heterolytic cleavage of the dihydrogen molecule. We have engineered a fusion of these two subunits. The resulting new enzyme showed no significant difference in hydrogen uptake activity or in the Ni-C or Ni-L EPR spectra compared to the the wild-type enzyme, but exhibited a tenfold increase in both the K m for hydrogen and the K i for the competitive inhibitor carbon monoxide.
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Bingemann, R., Pierik, A. & Klein, A. Influence of the fusion of two subunits of the F420-non-reducing hydrogenase of Methanococcus voltae on its biochemical properties. Arch Microbiol 174, 375–378 (2000). https://doi.org/10.1007/s002030000213
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DOI: https://doi.org/10.1007/s002030000213