Influence of heme environment structure on dioxygen affinity for the dual function Amphitrite ornata hemoglobin/dehaloperoxidase. Insights into the evolutional structure-function adaptations

Archives of Biochemistry and Biophysics

Volumn 545, Issue , 2014, Pages 108-115

  Sun, Shengfang ^a   Sono, Masanori ^a   Wang, Chunxue ^a   Du, Jing ^a   Lebioda, Lukasz ^a   Dawson, John H ^a,b  

^a UNIVERSITY OF SOUTH CAROLINA   (United States)

^b UNIVERSITY OF SOUTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

Amphitrite ornata dehaloperoxidase (DHP); Evolutional structure function adaptations; Heme environment mutants; Sperm whale myoglobin (Mb)

Indexed keywords

DEHALOPEROXIDASE; GLOBIN; HEMOGLOBIN; IRON; MYOGLOBIN; OXYGEN; PEROXIDASE; UNCLASSIFIED DRUG;

AMPHITRITE ORNATA; ARTICLE; CATALYSIS; ENZYME ACTIVITY; EQUILIBRIUM CONSTANT; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; SPERM WHALE; WORM;

AMPHITRITE ORNATA DEHALOPEROXIDASE (DHP); EVOLUTIONAL STRUCTURE-FUNCTION ADAPTATIONS; HEME ENVIRONMENT MUTANTS; O(2) AFFINITY; SPERM WHALE MYOGLOBIN (MB);

ANIMALS; CRYSTALLOGRAPHY, X-RAY; HEME; MODELS, MOLECULAR; MYOGLOBIN; OXYGEN; PEROXIDASES; POLYCHAETA; PROTEIN CONFORMATION; SPERM WHALE;

EID: 84893791776     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2014.01.010     Document Type: Article

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