The luciferases from three very distinct species of luminous bacteria, Beneckea , harveyi , Photobacterium , fischeri , and, Photobacterium , phosphoreum , bind phosphate and other anions to form complexes with decreased sensitivity to proteases and increased thermal stability. Upon treatment with either trypsin or chymotrypsin in either low phosphate or high phosphate buffers, the rate of loss of activity of all three luciferases is the same as the rate of bond cleavage within a discrete region of the α subunit. Unlike the enzyme from B. , harveyi , the β subunits of the enzymes from the Photobacterium species are sensitive to the proteases in low phosphate, while in high phosphate, the β subunits of all three luciferases are not sensitive to trypsin or chymotrypsin.