Mössbauer spectroscopy applied to the oxidized and semi-reduced states of the iron-molybdenum cofactor of nitrogenase
Mössbauer parameters at 125K for both the oxidized and semi-reduced states of FeMoco isolated from the MoFe protein of Azotobacter vinelandii nitrogenase of δ Fe =0.32 and 0.37 mm/s and ΔEq=0.84 and 0.71 mm/s, respectively, are reported. FeMoco(ox) fits the Debye model perfectly from 4.2–125K and ha...
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Published in | Biochemical and biophysical research communications Vol. 162; no. 2; pp. 882 - 891 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
San Diego, CA
Elsevier Inc
31.07.1989
Elsevier |
Subjects | |
Online Access | Get full text |
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