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Spectroscopic investigation of the nickel-containing porphinoid cofactor F-430. Comparison of the free cofactor in the +1, +2 and +3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms

MPS-Authors

Duin,  E. C.
Max Planck Society;

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Mahlert,  F.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Goenrich,  M.
Department of Biochemistry, Alumni, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Thauer,  R. K.
Emeriti Biochemistry of Anaerobic Microorganisms, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Duin, E. C., Signor, L., Piskorski, R., Mahlert, F., Clay, M. D., Goenrich, M., et al. (2004). Spectroscopic investigation of the nickel-containing porphinoid cofactor F-430. Comparison of the free cofactor in the +1, +2 and +3 oxidation states with the cofactor bound to methyl-coenzyme M reductase in the silent, red and ox forms. Journal of Biological Inorganic Chemistry, 9(5), 563-576.


Cite as: http://hdl.handle.net/21.11116/0000-0007-C902-4
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