참고문헌
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- The activity of nitrogenase is generally represented by how much electrons are transferred to substrates because all electrons transferred to MoFe protein are used for substrate reduction
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- Although 1Mo4+, 1Fe3+, 6Fe3+ model was suggested by ENDOR spectroscopic study, Yoo, et al's result is recently more supported.
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- Lee, H.-I., Benton, P. M. C., Laryukhin, M., Igarashi, R. Y., Dean, D. R., Seefeldt, L. C. and Hoffman, B. M. (2003) The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM show it is not an exchangeable nitrogen. J. Am. Chem. Soc. 125, 5604-5605 https://doi.org/10.1021/ja034383n
- The distances are very short, considering hydrogen atoms are bonded to the amino acid residues
- It is reported recently that the atom inside FeMo-cofactor may not be nitrogen atom. Yang, T.-C., Maeser, N. K., Laryukhin, M., Lee, H.-I., Dean, D. R., Seefeldt, L. C. and Hoffman, B. M. (2005) The interstitial atom of the nitrogenase FeMocofactor: ENDOR and ESEEM evidence that it is not a nitrogen. J. Am. Chem. Soc. ASAP ja0552489