TY - JOUR
T1 - Ligand binding equilibrium and kinetic measurements on the dimeric myoglobin of Busycon canaliculatum and the comparative ligand binding of diverse non-cooperative heme proteins
AU - Schreiber, Jane K.
AU - Parkhurst, Lawrence J.
N1 - Funding Information:
Acknon~ledgemenls-Support for this research was from NIH HL-15,284, NSF PCM 8003655, and the Research Council, University of Nebraska.
PY - 1984
Y1 - 1984
N2 - 1. 1. The rate constants and ΔH° for the non-cooperative dimeric Busycon myoglobin are: oxygen, k' = 4.75 × 107M-1, k = 71 sec-1, and CO, l′ -3.46 × 105 M-li]1sec-1, l = 0.0052 sec-1 at 20°C, pH 7. ΔH° = -3 kcal/mol for O2 and CO. 2. Log-log plots of k vs K for oxygen and of l′ vs L for CO binding for numerous non-cooperative hemoglobins and myoglobins point to a large steric influence of the protein on heme ligation reactions. Many of the proteins behave as "R" state for one ligand, but "T" for the other.
AB - 1. 1. The rate constants and ΔH° for the non-cooperative dimeric Busycon myoglobin are: oxygen, k' = 4.75 × 107M-1, k = 71 sec-1, and CO, l′ -3.46 × 105 M-li]1sec-1, l = 0.0052 sec-1 at 20°C, pH 7. ΔH° = -3 kcal/mol for O2 and CO. 2. Log-log plots of k vs K for oxygen and of l′ vs L for CO binding for numerous non-cooperative hemoglobins and myoglobins point to a large steric influence of the protein on heme ligation reactions. Many of the proteins behave as "R" state for one ligand, but "T" for the other.
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U2 - 10.1016/0300-9629(84)90104-X
DO - 10.1016/0300-9629(84)90104-X
M3 - Article
C2 - 6146431
AN - SCOPUS:0021187845
VL - 78
SP - 129
EP - 135
JO - Comparative Biochemistry and Physiology -- Part A: Physiology
JF - Comparative Biochemistry and Physiology -- Part A: Physiology
SN - 0300-9629
IS - 1
ER -