Identification of a thiol/disulfide redox switch in the human BK channel that controls its affinity for heme and CO

Journal of Biological Chemistry

Volumn 285, Issue 26, 2010, Pages 20117-20127

  Yi, Li ^a   Morgan, Jeffrey T ^a   Ragsdale, Stephen W ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMICAL EXPERIMENTS; BK-CHANNEL; CAROTID BODY; CYS RESIDUES; CYSTEINE RESIDUES; CYTOPLASMIC DOMAINS; DITHIOLS; HEME OXYGENASE-2; HEME-BINDING DOMAINS; MANY ELECTRON; NORMOXIC CONDITIONS; PROSTHETIC GROUPS; PROTEIN COMPLEXES; REDOX ENZYME; REDOX STATE; REDOX SWITCH;

CALCIUM; HEMOGLOBIN; OXYGEN; PHOSPHATASES;

PORPHYRINS;

DISULFIDE; HEME OXYGENASE 2; HEMOPROTEIN; LARGE CONDUCTANCE CALCIUM ACTIVATED POTASSIUM CHANNEL; THIOL;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ELECTROPHYSIOLOGY; HUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; SITE DIRECTED MUTAGENESIS; STOICHIOMETRY; T LYMPHOCYTE ACTIVATION;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; BINDING, COMPETITIVE; CARBON MONOXIDE; CYSTEINE; DISULFIDES; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FERRIC COMPOUNDS; FERROUS COMPOUNDS; HEME; HEME OXYGENASE (DECYCLIZING); HUMANS; LARGE-CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA SUBUNITS; MUTAGENESIS, SITE-DIRECTED; MUTATION; OXIDATION-REDUCTION; PROTEIN BINDING; SULFHYDRYL COMPOUNDS;

EID: 77953796852     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.116483     Document Type: Article

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