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• W2094787456 abstract "The alternative nitrogenase of Rhodobacter capsulatus, isolated from a nifHDK deletion mutant, has been purified to near homogeneity and identified as an 'iron only' nitrogenase. The dithionite-reduced component 1 ('FeFe protein') of this enzyme showed an EPR spectrum consisting of two components: a minor S = 1/2 signal at g = 1.93 and a very characteristic S = 3/2 signal of near-stoichiometric intensity at g = 5.44. This resonance is very close to the highest possible g value (g = 5.46) for the coinciding two intradoublet subspectra of an S = 3/2 system of maximal rhombicity (E/D = 0.33). The deviation from axial symmetry (increasing E/D) correlates with the stability, activity and substrate selectivity of the different (Mo, V, Fe) nitrogenases." @default.
• W2094787456 created "2016-06-24" @default.
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• W2094787456 date "1992-05-25" @default.
• W2094787456 modified "2023-10-14" @default.
• W2094787456 title "EPR spectroscopic characterization of an ‘iron only⌉ nitrogenase<i>S</i>= 3/2 spectrum of component 1 isolated from<i>Rhodobacter capsulatus</i>" @default.
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• W2094787456 doi "https://doi.org/10.1016/0014-5793(92)80472-s" @default.
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