Abstract
Sperm whale myoglobin, horse myoglobin, bovine hemoglobin, and human hemoglobin produced well-defined catalytic hydrogen current (Brdi_??_ka current) in buffer solutions containing cobalt salts at dme and hmde. The Brdi_??_ka current-activity of the myoglobins was shown to be due to the heme group and that of the hemoglobins to both the heme groups and SH groups in the molecule. The Brdicka current produced by human hemoglobin was reduced by the addition of 2, 3-diphosphoglycerate (DPG), indicating that the formation of a hemoglobin-DPG complex resulted in the reduction of the Brdicka current-activity of the protein.
