Structural Investigation of the Molybdenum Site of the Periplasmic Nitrate Reductase from Thiosphaera pantotropha by X-ray Absorption Spectroscopy

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Format of Original

7 p.

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Portland Press Limited

Source Publication

Biochemical Journal

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The molybdenum centre of the periplasmic respiratory nitrate reductase from the denitrifying bacterium Thiosphaera pantotropha has been probed using molybdenum K-edge X-ray absorption spectroscopy. The optimum fit of the Mo(VI) EXAFS suggests two O, three –S– and either a fourth –S– or an –O–/–N– as molybdenum ligands in the ferricyanide-oxidized enzyme. Three of the –S– ligands are proposed to be the two sulphur atoms of the molybdopterin dithiolene group and Cys-181. Comparison of the EXAFS of the ferricyanide-oxidized enzyme with that of a nitrate-treated sample containing 30% Mo(V) suggests that the Mo(VI) Mo(V) reduction is accompanied by conversion of one O to –O–. The best fit to the Mo(IV) EXAFS of dithionite-reduced enzyme was obtained using one O, one –O– and four –S–/–Cl ligands. The periplasmic nitrate reductase molybdenum co-ordination environment in both the Mo(VI) and Mo(IV) oxidation states is distinct from that found in the membrane-bound respiratory nitrate reductase.


Biochemical Journal, Vol. 317, No. 2 (July 15, 1996): 557-563. Permalink.

Brian Bennett was affiliated with the University of East Anglia at the time of publication.