The Disorganized personality

xiv, 476 p.; 23 cm

Structure of the active site of sulfite dehydrogenase from Starkeya novella

In this paper, we report the results of molybdenum K-edge X-ray absorption studies performed on the oxidized and reduced active sites of the sulfite dehydrogenase from Starkeya novella. Our results provide the first direct structural information on the active site of the oxidized form of this enzyme and confirm the conclusions derived from protein crystallography that the molybdenum coordination is analogous to that of the sulfite oxidases. The molybdenum atom of the oxidized enzyme is bound by two Mo=O ligands at 1.73 A and three thiolate Mo-S ligands at 2.42 A, whereas the reduced enzyme has one oxo at 1.74 A, one long oxygen at 2.19 A (characteristic of Mo-OH2), and three Mo-S ligands at 2.40 A.Christian J. Doonan, Ulrike Kappler and Graham N. Georg

Nature of halide binding to the molybdenum site of sulfite oxidase

Valuable information on the active sites of molybdenum enzymes has been provided from both Mo(V) electron paramagnetic resonance (EPR) spectroscopy and X-ray absorption spectroscopy (XAS). One of three major categories of Mo(V) EPR signals from the molybdenum enzyme sulfite oxidase is the low-pH signal, which forms in the presence of chloride. Two alternative structures for this species have been proposed, one in which the chloride is coordinated directly to Mo and a second in which chloride is held in the arginine-rich basic pocket some 5 Å from Mo. Here we present an independent assessment of the structure of this species by using XAS of the analogous bromide and iodide complexes. We show that there is no evidence of direct Mo-I coordination, and that the data are consistent with a structure in which the halide is bound at ∼5 Å from Mo.M. Jake Pushie, Christian J. Doonan, Heather L. Wilson, K. V. Rajagopalan, and Graham. N. Georg