Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme

Biochemistry

Volumn 54, Issue 17, 2015, Pages 2693-2708

  Bagai, Ireena ^a   Sarangi, Ritimukta ^b   Fleischhacker, Angela S ^a   Sharma, Ajay ^c   Hoffman, Brian M ^c   Zuiderweg, Erik R P ^a   Ragsdale, Stephen W ^a  

^a UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

^c NORTHWESTERN UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION SPECTROSCOPY; AMINO ACIDS; MOBILE SECURITY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PORPHYRINS; SPECTROSCOPIC ANALYSIS; X RAY ABSORPTION; X RAY ABSORPTION SPECTROSCOPY;

C-TERMINAL REGIONS; ELECTRON NUCLEAR DOUBLE RESONANCE; HEME REGULATORY MOTIFS; NADPH-CYTOCHROME P450 REDUCTASE; PROSTHETIC GROUPS; REDUCING CONDITIONS; SPECTROSCOPIC STUDIES; SPECTROSCOPIC TECHNIQUE;

ELECTRON SPIN RESONANCE SPECTROSCOPY;

CYSTEINE; HEME; HEME OXYGENASE 2; IRON; HEME OXYGENASE; HEME OXYGENASE-2;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CHEMICAL COMPOSITION; CRYSTAL STRUCTURE; ELECTRON NUCLEAR DOUBLE RESONANCE; ELECTROSPRAY MASS SPECTROMETRY; HETERONUCLEAR SINGLE QUANTUM COHERENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTON NUCLEAR MAGNETIC RESONANCE; AMINO ACID SEQUENCE; CHEMISTRY; METABOLISM; MOLECULAR GENETICS; OXIDATION REDUCTION REACTION; PROCEDURES; SEQUENCE HOMOLOGY; SPECTROSCOPY;

MAMMALIA;

AMINO ACID SEQUENCE; HEME; HEME OXYGENASE (DECYCLIZING); MOLECULAR SEQUENCE DATA; OXIDATION-REDUCTION; SEQUENCE HOMOLOGY, AMINO ACID; SPECTRUM ANALYSIS;

EID: 84928944221     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi501489r     Document Type: Article

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