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Publikováno v:
Biochemistry. 45:9706-9716
The active site in the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F has been investigated by Fourier transform infrared (FTIR) spectroscopy. Analysis of the spectra allowed the three diatomic inorganic ligands to Fe in this enzyme to be id
Publikováno v:
Phys. Chem. Chem. Phys.. 5:5507-5513
The conversion process of the Ni–C to the Ni–L redox state of the [NiFe] center in Desulfovibrio vulgaris Miyazaki F hydrogenase is investigated by EPR spectroscopy following laser excitation at distinct wavelengths. The Ni–L state is character
Publikováno v:
Physical Chemistry Chemical Physics (PCCP); Dec2003, Vol. 5 Issue 24, p5507-5513, 7p
Publikováno v:
ResearcherID
Isolation and purification of the [NiFe] hydrogenase of Desulfovibrio vulgaris Miyazaki F under aerobic conditions leads to a mixture of two states, Ni-A (unready) and Ni-B (ready). The two states are distinguished by different activation times and d
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