Ligand binding equilibrium and kinetic measurements on the dimeric myoglobin of Busycon canaliculatum and the comparative ligand binding of diverse non-cooperative heme proteins

Jane K. Schreiber, Lawrence J Parkhurst

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)129-135
Number of pages7
JournalComparative Biochemistry and Physiology -- Part A: Physiology
Volume78
Issue number1
DOIs
StatePublished - 1984

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Hemeproteins
Myoglobin
Carbon Monoxide
Ligands
Kinetics
Oxygen
Heme
Ligation
Rate constants
Hemoglobins
Proteins

ASJC Scopus subject areas

  • Physiology

Cite this

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title = "Ligand binding equilibrium and kinetic measurements on the dimeric myoglobin of Busycon canaliculatum and the comparative ligand binding of diverse non-cooperative heme proteins",
abstract = "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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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

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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