Hydrogen-bonding conformations of tyrosine B10 tailor the hemeprotein reactivity of ferryl species

Journal of Biological Inorganic Chemistry

Volumn 11, Issue 3, 2006, Pages 334-342

  De Jesús Bonilla, Walleska ^a   Cruz, Anthony ^a   Lewis, Ariel ^a   Cerda, José ^d   Bacelo, Daniel E ^b   Cadilla, Carmen L ^c   López Garriga, Juan ^a  

^a UNIVERSITY OF PUERTO RICO   (Puerto Rico)

^b UNIVERSIDAD METROPOLITANA   (Puerto Rico)

^c UNIVERSITY OF PUERTO RICO SCHOOL OF MEDICINE   (Puerto Rico)

^d UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Ferryl species; Hydrogen peroxide; Lucina pectinata hemoglobins; Proximal HisF8 trans effect; Tyrosine B10

Indexed keywords

AMINO ACID; GLUTAMINE; HEMOGLOBIN; HEMOGLOBIN II; HEMOPROTEIN; HYDROGEN PEROXIDE; IRON DERIVATIVE; MUTANT PROTEIN; PHENYLALANINE; RECOMBINANT HEMOGLOBIN; RECOMBINANT HEMOGLOBIN I; TYROSINE; TYROSINE B10; TYROSINE DERIVATIVE; UNCLASSIFIED DRUG;

AEROBIC METABOLISM; ARTICLE; CATALYSIS; CLAM; CONFORMATION; ENZYME ACTIVITY; HYDROGEN BOND; LUCINA PECTINATA; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DEGRADATION; ULTRAVIOLET RADIATION;

FERRIC COMPOUNDS; HEMOGLOBINS; HYDROGEN BONDING; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; KINETICS; TYROSINE;

BIVALVIA; LUCINA PECTINATA;

EID: 33645532799     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00775-006-0082-0     Document Type: Article

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