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By Dunitz J.D.

ISBN-10: 354007886X

ISBN-13: 9783540078869

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Extra resources for Structure and Bonding, Vol. 29

Example text

This metal has also been used to replace Mo in Azotobacter MoFe protein (91). Co-purification of W with nitrogenase activity was found to a limiting 42 The MolecularBasis of BiologicalDinitrogen Fixation extent and the resulting enzyme preparation showed strong inhibition of C2H2 reduction, H 2 evolution, and ATP hydrolysis. Traces of Mo might again account for this residual activity, since the acetylene-reducing activity of the W analogue could not be confirmed (19 7). Molybdenum appears generally to be replaceable by W in Mo-containing enzymes such as nitrate reductase (199), sulfite oxidase (200), or xanthine oxidase (201).

Claims on electron transfer rates or rate-limiting reactions should be viewed with caution as long as these discrepancies remain unresolved. However, there is an agreement on the overall phenomena of signal decline and reappearance under defined reducing or oxidizing conditions (54, 55, 56, 190). When reductant is limiting and dithionite is being exhausted by dinitrogen evolution, the EPR signal of the MoFe protein returns to its original state, whereas the signal of the Fe protein disappears completely (Fig.

Biochem. Soc. from Ref. (56). Table 6. 5 Data are taken from Refs. (56) and (186). G. Zumft The transition induced by Mg. ATP in the EPR spectrum of the Fe protein, which was related to a conformational change, could also be related to a change in the redox potential (56). In the presence of Mg. 5; Fig. 6). Since the Fe protein under turnover conditions of the nitrogenase reaction is present in its ATP form, this lower redox potential appears to be effective in the catalytic cycle of the enzyme.

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Structure and Bonding, Vol. 29 by Dunitz J.D.

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