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

FEBS Letters

Volumn 589, Issue 4, 2015, Pages 507-512

  Beckerson, Penny ^a   Reeder, Brandon J ^a   Wilson, Michael T ^a  

^a UNIVERSITY OF ESSEX   (United Kingdom)

Author keywords

Biphasic; Carbon monoxide; Cysteine; Cytoglobin; Dimer; Distal histidine; Disulfide; Ferrous; Flash photolysis; Monomer

Indexed keywords

CARBON MONOXIDE; COORDINATION COMPOUND; CYSTEINE; CYTOGLOBIN; DIMER; HEXACOORDINATE; HISTIDINE; MONOMER; PENTACOORDINATE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CHEMICAL BINDING; COMPLEX FORMATION; CONCENTRATION (PARAMETERS); CROSS LINKING; DISSOCIATION CONSTANT; DISTAL HISTIDINE DISSOCIATION; DISULFIDE BOND; HUMAN; LIGAND BINDING; OXIDATION REDUCTION STATE; PHOTOLYSIS; PROTEIN FUNCTION; PROTEIN STRUCTURE; STOICHIOMETRY;

EID: 84964253278     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.01.010     Document Type: Article

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