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Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding

•An intramolecular disulfide bond in monomeric cytoglobin modulates CO binding.•Histidine on and off rates for the different forms of cytoglobin were determined.•We identify two forms of the hexacoordinate monomeric protein.•A model is presented describing CO binding to the different forms of cytogl... Full description

Journal Title: FEBS Letters 13 February 2015, Vol.589(4), pp.507-512
Main Author: Beckerson, Penny
Other Authors: Reeder, Brandon J , Wilson, Michael T
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2015.01.010
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recordid: elsevier_sdoi_10_1016_j_febslet_2015_01_010
title: Coupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding
format: Article
creator:
  • Beckerson, Penny
  • Reeder, Brandon J
  • Wilson, Michael T
subjects:
  • Cytoglobin
  • Carbon Monoxide
  • Flash Photolysis
  • Ferrous
  • Biphasic
  • Distal Histidine
  • Monomer
  • Dimer
  • Disulfide
  • Cysteine
  • Cytoglobin
  • Carbon Monoxide
  • Flash Photolysis
  • Ferrous
  • Biphasic
  • Distal Histidine
  • Monomer
  • Dimer
  • Disulfide
  • Cysteine
ispartof: FEBS Letters, 13 February 2015, Vol.589(4), pp.507-512
description: •An intramolecular disulfide bond in monomeric cytoglobin modulates CO binding.•Histidine on and off rates for the different forms of cytoglobin were determined.•We identify two forms of the hexacoordinate monomeric protein.•A model is presented describing CO binding to the different forms of cytoglobin. Earlier kinetics studies on cytoglobin did not assign functional properties to specific structural forms. Here, we used defined monomeric and dimeric forms and cysteine mutants to show that an intramolecular disulfide bond (C38–C83) alters the dissociation rate constant of the intrinsic histidine (H81) (∼1000fold), thus controlling binding of extrinsic ligands. Through time-resolved spectra we have unequivocally assigned CO binding to hexa- and penta-coordinate forms and have made direct measurement of histidine rebinding following photolysis. We present a model that describes how the cysteine redox state of the monomer controls histidine dissociation rate constants...
language: eng
source:
identifier: ISSN: 0014-5793 ; E-ISSN: 1873-3468 ; DOI: 10.1016/j.febslet.2015.01.010
fulltext: fulltext
issn:
  • 0014-5793
  • 00145793
  • 1873-3468
  • 18733468
url: Link


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titleCoupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding
creatorBeckerson, Penny ; Reeder, Brandon J ; Wilson, Michael T
ispartofFEBS Letters, 13 February 2015, Vol.589(4), pp.507-512
identifier
subjectCytoglobin ; Carbon Monoxide ; Flash Photolysis ; Ferrous ; Biphasic ; Distal Histidine ; Monomer ; Dimer ; Disulfide ; Cysteine ; Cytoglobin ; Carbon Monoxide ; Flash Photolysis ; Ferrous ; Biphasic ; Distal Histidine ; Monomer ; Dimer ; Disulfide ; Cysteine
description•An intramolecular disulfide bond in monomeric cytoglobin modulates CO binding.•Histidine on and off rates for the different forms of cytoglobin were determined.•We identify two forms of the hexacoordinate monomeric protein.•A model is presented describing CO binding to the different forms of cytoglobin. Earlier kinetics studies on cytoglobin did not assign functional properties to specific structural forms. Here, we used defined monomeric and dimeric forms and cysteine mutants to show that an intramolecular disulfide bond (C38–C83) alters the dissociation rate constant of the intrinsic histidine (H81) (∼1000fold), thus controlling binding of extrinsic ligands. Through time-resolved spectra we have unequivocally assigned CO binding to hexa- and penta-coordinate forms and have made direct measurement of histidine rebinding following photolysis. We present a model that describes how the cysteine redox state of the monomer controls histidine dissociation rate constants...
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titleCoupling of disulfide bond and distal histidine dissociation in human ferrous cytoglobin regulates ligand binding
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•An intramolecular disulfide bond in monomeric cytoglobin modulates CO binding.•Histidine on and off rates for the different forms of cytoglobin were determined.•We identify two forms of the hexacoordinate monomeric protein.•A model is presented describing CO binding to the different forms of cytoglobin.

Earlier kinetics studies on cytoglobin did not assign functional properties to specific structural forms. Here, we used defined monomeric and dimeric forms and cysteine mutants to show that an intramolecular disulfide bond (C38–C83) alters the dissociation rate constant of the intrinsic histidine (H81) (∼1000fold), thus controlling binding of extrinsic ligands. Through time-resolved spectra we have unequivocally assigned CO binding to hexa- and penta-coordinate forms and have made direct measurement of histidine rebinding following photolysis. We present a model that describes how the cysteine redox state of the monomer controls histidine dissociation rate constants...

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abstract

•An intramolecular disulfide bond in monomeric cytoglobin modulates CO binding.•Histidine on and off rates for the different forms of cytoglobin were determined.•We identify two forms of the hexacoordinate monomeric protein.•A model is presented describing CO binding to the different forms of cytoglobin.

Earlier kinetics studies on cytoglobin did not assign functional properties to specific structural forms. Here, we used defined monomeric and dimeric forms and cysteine mutants to show that an intramolecular disulfide bond (C38–C83) alters the dissociation rate constant of the intrinsic histidine (H81) (∼1000fold), thus controlling binding of extrinsic ligands. Through time-resolved spectra we have unequivocally assigned CO binding to hexa- and penta-coordinate forms and have made direct measurement of histidine rebinding following photolysis. We present a model that describes how the cysteine redox state of the monomer controls histidine dissociation rate constants...

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