Abstract
We have used the Mössbauer effect to study the found in the active centers of two enzymes, cytochome c and putidaredoxin. The temperature dependence and magnitude of the quadrupole splitting of cytochome c are interpreted in terms of molecular orbitals. The Mössbauer spectra of putidaredoxin show that the two iron atoms of that molecule are identical and one electron reduces both. The Mössbauer data are correlated with the results of electron-spin resonance and magnetic susceptibility experiments and are discussed in terms of models of the active site.
Supported by the National Institute of Health, 5T1-GM720 and the U.S. Office of Naval Research under Contract 00014-67-A-0305-0005.
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Cooke, R. (1968). Enzyme Studies with the Mössbauer Effect. In: Gruverman, I.J. (eds) Mössbauer Effect Methodology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1550-7_7
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DOI: https://doi.org/10.1007/978-1-4757-1550-7_7
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