Crystal structures of Parasponia and trema hemoglobins: Differential heme coordination is linked to quaternary structure

Biochemistry

Volumn 50, Issue 20, 2011, Pages 4273-4280

  Kakar, Smita ^a   Sturms, Ryan ^a   Tiffany, Andrea ^a   Nix, Jay C ^b   Dispirito, Alan A ^a   Hargrove, Mark S ^a  

^a IOWA STATE UNIVERSITY   (United States)

^b LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CLASS 1; MUTANT PROTEINS; OXIDATION STATE; OXYGEN BINDING; PHYSIOLOGICAL FUNCTIONS; PLANT OXYGEN TRANSPORT; POTENTIAL FUNCTION; PRIMARY STRUCTURES; QUATERNARY STRUCTURE; REDOX POTENTIALS; SEQUENCE IDENTITY; SIDE-CHAINS; STRUCTURAL HETEROGENEITY; SUBUNIT HETEROGENEITY; WILD TYPES;

CRYSTAL STRUCTURE; OXYGEN; PORPHYRINS; PROTEINS; REDOX REACTIONS;

HEMOGLOBIN;

HEME; HEMOGLOBIN; MUTANT PROTEIN;

ARTICLE; CRYSTAL STRUCTURE; OXIDATION REDUCTION REACTION; PARASPONIA ANDERSONII; PLANT; PRIORITY JOURNAL; PROTEIN QUATERNARY STRUCTURE; SEQUENCE ANALYSIS; SYMBIOSIS; TREMA TOMENTOSA; WILD TYPE; X RAY CRYSTALLOGRAPHY;

BIOLOGICAL TRANSPORT; CRYSTALLOGRAPHY, X-RAY; HEME; HEMOGLOBINS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; OXYGEN; PLANT PROTEINS; PROTEIN STRUCTURE, QUATERNARY; PROTEIN SUBUNITS; TREMA;

PARASPONIA; PARASPONIA ANDERSONII; TREMA; TREMA TOMENTOSA;

EID: 79956222405     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi2002423     Document Type: Article

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