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• W2056553456 abstract "Computer simulated spectra are calculated and compared with experimental E.S.R. spectra for vitamin B12r (cob(II)alamin) in the enzyme ribonucleotide reductase. The conclusions reached are that the cobalt(II) ion in the corrinoid is in a site of no higher than C 2 point group symmetry; that the cobalt g and hyperfine tensors are non-coincident, sharing the z-axis, but with their axes in the xy plane rotated 50° with respect to one another. The unpaired electron is still considered to be in an essentially d z 2 orbital, though a certain amount of mixing of states is thought to occur, accounting for the non-coincidence of the tensors. As an aid to our analysis, we present results for two model systems, firstly pentacyanocobaltate(II) ion, where close agreement with the work of Tsay, Gray and Danon is found, and secondly pentacyanocobaltate(II) ion with pyridine in the sixth coordination position." @default.
• W2056553456 created "2016-06-24" @default.
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• W2056553456 date "1973-05-01" @default.
• W2056553456 modified "2023-09-28" @default.
• W2056553456 title "Computer simulation of low symmetry E.S.R. spectra due to vitamin B_12rand model systems" @default.
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• W2056553456 doi "https://doi.org/10.1080/00268977300100941" @default.
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