Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis

Biochemistry

Volumn 46, Issue 27, 2007, Pages 7973-7979

  Dailey, Harry A ^a,b   Wu, Chia Kuei ^b   Horanyi, Peter ^b   Medlock, Amy E ^a,b   Najahi Missaoui, Wided ^b   Burden, Amy E ^b   Dailey, Tamara A ^a,b   Rose, John ^b  

^a Paul D Coverdell Center for Biomedical and Health Sciences   (United States)

^b University of Georgia ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN FERROCHELATASE; PORPHYRIN MACROCYCLE; PROTOPORPHYRIN SUBSTRATE;

AMINO ACIDS; BIOSYNTHESIS; CATALYSIS; CRYSTAL STRUCTURE; HYDROGEN BONDS; PORPHYRINS; SUBSTITUTION REACTIONS;

ENZYME KINETICS;

AMINO ACID; FERROCHELATASE; FERROUS ION; HEME; MACROCYCLIC COMPOUND; NITROGEN; PORPHYRIN; PROTOPORPHYRIN; PYRROLE;

AMINO ACID SUBSTITUTION; ARTICLE; BIOSYNTHESIS; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GENE DISRUPTION; GENETIC VARIABILITY; HUMAN; HYDROGEN BOND; PRIORITY JOURNAL;

BINDING SITES; CATALYSIS; FERROCHELATASE; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR;

EID: 34447311943     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700151f     Document Type: Article

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