Oxymyohemerythrin: Discriminating between O2 release and autoxidation

Christopher R. Lloyd, Gregory M. Raner, Alicia Moser, Edward M. Eyring, Walther R Ellis

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Myohemerythrin (Mhr) is a non-heme iron O2 carrier (with two irons in the active site) that is typically found in the retractor muscle of marine 'peanut' worms. OxyMhr may either release O2, or undergo an autoxidation reaction in which hydrogen peroxide is released and diferric metMhr is produced. The autoxidation reaction can also be promoted by the addition of certain anions to Mhr solutions. This work, using recombinant Themiste zostericola Mhrs, contrasts the results of environmental effects on these reactions. For the O2 release reaction, ΔV(Double Dagger) (21.5°C)=+28±3 cm3mol-1, ΔH(Double Dagger) (1 atm)=+22±1 kcalmol-1, and ΔS(Double Dagger) (1 atm)=+ 28±4 eu. The autoxidation reaction (pH 8.0, 21.5°C, 1 atm) displays different kinetic parameters: ΔVDouble Dagger)= -8±2 cm3mol-1, ΔH(Double Dagger)=+24.1±0.7 kcalmol-1, and ΔS(Double Dagger)=+1±1 eu. Autoxidation in the presence of sodium azide is orders of magnitude faster than solvolytic autoxidation. The ΔV(Double Dagger) parameters for azide anation and azide-assisted autoxidation reaction are +15±2 and +59±2 cm3mol-1, respectively, indicating that the rate-limiting steps for the Mhr autoxidation and anation reactions (including O2 uptake) are not associated with ligand binding to the Fe2 center. The L103V and L103N oxyMhr mutants autoxidize ~103-105 times faster than the wild-type protein, emphasizing the importance of leucine-103, which may function as a protein 'gate' in stabilizing bound dioxygen. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)293-300
Number of pages8
JournalJournal of Inorganic Biochemistry
Volume81
Issue number4
DOIs
StatePublished - Oct 1 2000
Externally publishedYes

Fingerprint

Azides
Sodium Azide
Kinetic parameters
Leucine
Hydrogen Peroxide
Anions
Environmental impact
Muscle
Catalytic Domain
Proteins
Iron
Oxygen
Ligands
Muscles
myohemerythrin
oxymyohemerythrin
Arachis

Keywords

  • Autoxidation
  • Kinetics
  • Myohemerythrin
  • Non-heme iron

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

Cite this

Oxymyohemerythrin : Discriminating between O2 release and autoxidation. / Lloyd, Christopher R.; Raner, Gregory M.; Moser, Alicia; Eyring, Edward M.; Ellis, Walther R.

In: Journal of Inorganic Biochemistry, Vol. 81, No. 4, 01.10.2000, p. 293-300.

Research output: Contribution to journalArticle

Lloyd, Christopher R. ; Raner, Gregory M. ; Moser, Alicia ; Eyring, Edward M. ; Ellis, Walther R. / Oxymyohemerythrin : Discriminating between O2 release and autoxidation. In: Journal of Inorganic Biochemistry. 2000 ; Vol. 81, No. 4. pp. 293-300.
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abstract = "Myohemerythrin (Mhr) is a non-heme iron O2 carrier (with two irons in the active site) that is typically found in the retractor muscle of marine 'peanut' worms. OxyMhr may either release O2, or undergo an autoxidation reaction in which hydrogen peroxide is released and diferric metMhr is produced. The autoxidation reaction can also be promoted by the addition of certain anions to Mhr solutions. This work, using recombinant Themiste zostericola Mhrs, contrasts the results of environmental effects on these reactions. For the O2 release reaction, ΔV(Double Dagger) (21.5°C)=+28±3 cm3mol-1, ΔH(Double Dagger) (1 atm)=+22±1 kcalmol-1, and ΔS(Double Dagger) (1 atm)=+ 28±4 eu. The autoxidation reaction (pH 8.0, 21.5°C, 1 atm) displays different kinetic parameters: ΔVDouble Dagger)= -8±2 cm3mol-1, ΔH(Double Dagger)=+24.1±0.7 kcalmol-1, and ΔS(Double Dagger)=+1±1 eu. Autoxidation in the presence of sodium azide is orders of magnitude faster than solvolytic autoxidation. The ΔV(Double Dagger) parameters for azide anation and azide-assisted autoxidation reaction are +15±2 and +59±2 cm3mol-1, respectively, indicating that the rate-limiting steps for the Mhr autoxidation and anation reactions (including O2 uptake) are not associated with ligand binding to the Fe2 center. The L103V and L103N oxyMhr mutants autoxidize ~103-105 times faster than the wild-type protein, emphasizing the importance of leucine-103, which may function as a protein 'gate' in stabilizing bound dioxygen. Copyright (C) 2000 Elsevier Science B.V.",
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