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 angstrom from Mo. Here we present an independent assessment of the structure of this species by using)(AS 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 similar to 5 angstrom from Mo.