Publications

hydrogen bonding of sulfur ligands in blue copper and iron-sulfur proteins: detection by resonance raman spectroscopy.	the resonance raman spectrum of the blue copper protein azurin from alcaligenes denitrificans exhibits nine vibrational modes between 330 and 460 cm-1, seven of which shift 0.4-3.0 cm-1 to lower energy after incubation of the protein in d2o. these deuterium-dependent shifts have been previously ascribed to exchangeable protons on imidazole ligands [nestor, l., larrabee, j. a., woolery, g., reinhammar, b., & spiro, t. g. (1984) biochemistry 23, 1084] or to exchangeable protons on amide groups whi ...	1987	3442645
characterization of d-aminoacylase from alcaligenes denitrificans da181.	the d-aminoacylase produced by alcaligenes denitrificans da181 was a new type of aminoacylase which had both high stereospecificity and specific activity. the molecular weight and isoelectric point of this enzyme were 58,000 and 4.4, respectively. the apparent km and kcat values of this enzyme for n-acetyl-d-methionine were estimated to be 0.48 mm and 6.24 x 10(4) min-1, respectively. the optimum temperature was 45 degrees c. the enzyme was stable up to 55 degrees c for 1 hr in the presence of 0 ...	1992	1368943