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By Tokunaga Sh.

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A) resulting in altered substrate affinity (152, 153), and indirect evidence from chemical models (6) indicate an involvement of Mo and therefore the MoFe protein in substrate binding. The electron-transfer sequence derived from EPR and M6ssbauer spectroscopy indicates that the MoFe protein acts as a terminal electron acceptor from where reducing equivalents are transferred to substrates. The appearance of a new EPR signal of the MoFe protein in the presence of CO (154) indicates that CO interacts with this protein.

118). Figure 4 depicts graphically the proposed multiple-site structure of nitrogenase as outlined above. Most of the experimental evidence suggests that these sites are located on the MoFe protein. Replacement of Mo by V (see Section VI. A) resulting in altered substrate affinity (152, 153), and indirect evidence from chemical models (6) indicate an involvement of Mo and therefore the MoFe protein in substrate binding. The electron-transfer sequence derived from EPR and M6ssbauer spectroscopy indicates that the MoFe protein acts as a terminal electron acceptor from where reducing equivalents are transferred to substrates.

Clostridial MoFe protein did not exhibit such a low potential component. Since dithionite reduces the MoFe protein of Clostridium and Klebsiella only sluggishly, incomplete equilibration as a result may cause the biphasic nature of the redox titration. G. 5 o I I I I ON~ Ioo 5o EPR SIGNAL HEIGHT(%) Fig. 5. Redox titration of the MoFe protein and its demolybdo form. (A) Titration of the MoFe protein (70 uM) in a solution of nine mediators (Em7 range - 325 to + 135 mV) with a saturated solution of thionine.

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A Cellular Triangle Containing a Specified Point by Tokunaga Sh.


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