Electron Paramagnetic Resonance (EPR) Studies on Hydrogenase-1 (HYD1) Purified from a Mutant Strain (AP6) ofEscherichia coliEnhanced in HYD1
Hydrogenase-1 (HYD1), overexpressed by twofold, has been purified to homogeneity and to a high specific activity from a mutant strain (AP6) ofEscherichia coliwhich lacks hydrogenase-2. Plasma emission spectroscopy indicated that 0.93 atom of nickel and 11.4 iron atoms were present in HYD1. EPR studi...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1996-10, Vol.227 (1), p.211-215 |
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| container_title | Biochemical and biophysical research communications |
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| creator | DerVartanian, M.E. Menon, N.K. Przybyla, A.E. Peck, Jr, H.D. DerVartanian, D.V. |
| description | Hydrogenase-1 (HYD1), overexpressed by twofold, has been purified to homogeneity and to a high specific activity from a mutant strain (AP6) ofEscherichia coliwhich lacks hydrogenase-2. Plasma emission spectroscopy indicated that 0.93 atom of nickel and 11.4 iron atoms were present in HYD1. EPR studies on the as isolated HYD1 detected a complex 3Fe-4S signal and a Ni(III) species. Reduction with hydrogen gas caused disappearance of both the 3Fe–4S cluster and initial Ni(III) signals. At the same time the EPR signature (small g=2.19 signal) of the activated hydrogenase appeared. The detection of a 4Fe–4S cluster signal was noted. Reduction of HYD1 with sodium dithionite caused all nickel signals to disappear. The 4Fe–4S complex intensity was slightly increased. The EPR responses in the three oxidation-reduction states are consistent with other known (NiFe)-hydrogenases. |
| doi_str_mv | 10.1006/bbrc.1996.1491 |
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Plasma emission spectroscopy indicated that 0.93 atom of nickel and 11.4 iron atoms were present in HYD1. EPR studies on the as isolated HYD1 detected a complex 3Fe-4S signal and a Ni(III) species. Reduction with hydrogen gas caused disappearance of both the 3Fe–4S cluster and initial Ni(III) signals. At the same time the EPR signature (small g=2.19 signal) of the activated hydrogenase appeared. The detection of a 4Fe–4S cluster signal was noted. Reduction of HYD1 with sodium dithionite caused all nickel signals to disappear. The 4Fe–4S complex intensity was slightly increased. 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Plasma emission spectroscopy indicated that 0.93 atom of nickel and 11.4 iron atoms were present in HYD1. EPR studies on the as isolated HYD1 detected a complex 3Fe-4S signal and a Ni(III) species. Reduction with hydrogen gas caused disappearance of both the 3Fe–4S cluster and initial Ni(III) signals. At the same time the EPR signature (small g=2.19 signal) of the activated hydrogenase appeared. The detection of a 4Fe–4S cluster signal was noted. Reduction of HYD1 with sodium dithionite caused all nickel signals to disappear. The 4Fe–4S complex intensity was slightly increased. The EPR responses in the three oxidation-reduction states are consistent with other known (NiFe)-hydrogenases.</abstract><pub>Elsevier Inc</pub><doi>10.1006/bbrc.1996.1491</doi><tpages>5</tpages></addata></record> |
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| title | Electron Paramagnetic Resonance (EPR) Studies on Hydrogenase-1 (HYD1) Purified from a Mutant Strain (AP6) ofEscherichia coliEnhanced in HYD1 |
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