Picosecond geminate recombination of CO to the complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin

Estelle Leclerc-L'Hostis; Stefan Franzen; Jean Christophe Lambry; Jean Louis Martin; Liliane Leclerc; Claude Poyart; Michael C. Marden

doi:10.1016/0167-4838(95)00237-5

Picosecond geminate recombination of CO to the complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin

Estelle Leclerc-L'Hostis
, Stefan Franzen
, Jean Christophe Lambry
, Jean Louis Martin
, Liliane Leclerc
, Claude Poyart
, Michael C. Marden

Research output: Contribution to journal › Article › peer-review

Abstract

Picosecond CO recombination kinetics have been measured after photodissociation of the artificial complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin. These systems show an enhancement of the geminate fraction of kinetics relative to unbound heme-CO, due in part to fast geminate kinetics (τ = 50 ps for the initial phase), as well as a decrease in the rate of migration of CO away from the binding site. This indicates that calmodulin provides a complete pocket around the heme group. Rather than competing with the hemes for binding to calmodulin, the melittin seems to act as a cap to further enclose the hemes; melittin increases the affinity of calmodulin for heme-CO, but only weakly affects the CO recombination kinetics.

Original language	English
Pages (from-to)	140-146
Number of pages	7
Journal	Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume	1293
Issue number	1
DOIs	https://doi.org/10.1016/0167-4838(95)00237-5
Publication status	Published - 7 Mar 1996
Externally published	Yes

Keywords

Calmodulin
Geminate kinetics
Heme pocket
Melittin

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10.1016/0167-4838(95)00237-5

Cite this

@article{0165619079ec4b72bee1760af1aef345,

title = "Picosecond geminate recombination of CO to the complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin",

abstract = "Picosecond CO recombination kinetics have been measured after photodissociation of the artificial complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin. These systems show an enhancement of the geminate fraction of kinetics relative to unbound heme-CO, due in part to fast geminate kinetics (τ = 50 ps for the initial phase), as well as a decrease in the rate of migration of CO away from the binding site. This indicates that calmodulin provides a complete pocket around the heme group. Rather than competing with the hemes for binding to calmodulin, the melittin seems to act as a cap to further enclose the hemes; melittin increases the affinity of calmodulin for heme-CO, but only weakly affects the CO recombination kinetics.",

keywords = "Calmodulin, Geminate kinetics, Heme pocket, Melittin",

author = "Estelle Leclerc-L'Hostis and Stefan Franzen and Lambry, \{Jean Christophe\} and Martin, \{Jean Louis\} and Liliane Leclerc and Claude Poyart and Marden, \{Michael C.\}",

year = "1996",

month = mar,

day = "7",

doi = "10.1016/0167-4838(95)00237-5",

language = "English",

volume = "1293",

pages = "140--146",

journal = "Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology",

issn = "0167-4838",

number = "1",

}

Picosecond geminate recombination of CO to the complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin. / Leclerc-L'Hostis, Estelle; Franzen, Stefan; Lambry, Jean Christophe et al.
In: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, Vol. 1293, No. 1, 07.03.1996, p. 140-146.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Picosecond geminate recombination of CO to the complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin

AU - Leclerc-L'Hostis, Estelle

AU - Franzen, Stefan

AU - Lambry, Jean Christophe

AU - Martin, Jean Louis

AU - Leclerc, Liliane

AU - Poyart, Claude

AU - Marden, Michael C.

PY - 1996/3/7

Y1 - 1996/3/7

N2 - Picosecond CO recombination kinetics have been measured after photodissociation of the artificial complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin. These systems show an enhancement of the geminate fraction of kinetics relative to unbound heme-CO, due in part to fast geminate kinetics (τ = 50 ps for the initial phase), as well as a decrease in the rate of migration of CO away from the binding site. This indicates that calmodulin provides a complete pocket around the heme group. Rather than competing with the hemes for binding to calmodulin, the melittin seems to act as a cap to further enclose the hemes; melittin increases the affinity of calmodulin for heme-CO, but only weakly affects the CO recombination kinetics.

AB - Picosecond CO recombination kinetics have been measured after photodissociation of the artificial complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin. These systems show an enhancement of the geminate fraction of kinetics relative to unbound heme-CO, due in part to fast geminate kinetics (τ = 50 ps for the initial phase), as well as a decrease in the rate of migration of CO away from the binding site. This indicates that calmodulin provides a complete pocket around the heme group. Rather than competing with the hemes for binding to calmodulin, the melittin seems to act as a cap to further enclose the hemes; melittin increases the affinity of calmodulin for heme-CO, but only weakly affects the CO recombination kinetics.

KW - Calmodulin

KW - Geminate kinetics

KW - Heme pocket

KW - Melittin

U2 - 10.1016/0167-4838(95)00237-5

DO - 10.1016/0167-4838(95)00237-5

M3 - Article

C2 - 8652619

AN - SCOPUS:0029872593

SN - 0167-4838

VL - 1293

SP - 140

EP - 146

JO - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

JF - Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

IS - 1

ER -

Picosecond geminate recombination of CO to the complexes calmodulin * heme-CO and calmodulin * heme-CO * melittin

Abstract

Keywords

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