Essential Amino Acid Residues Controlling the Unique Regioselectivity of Heme Oxygenase in Pseudomonas aeruginosa

Journal of the American Chemical Society

Volumn 126, Issue 14, 2004, Pages 4466-4467

  Fujii, Hiroshi ^a   Zhang, Xuhong ^b   Yoshida, Tadashi ^b  

^a INSTITUTE FOR MOLECULAR SCIENCE   (Japan)

^b YAMAGATA UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BILIVERDIN; CARBON MONOXIDE; HEME; HEME OXYGENASE; IRON; LYSINE; PHENYLALANINE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DEGRADATION; HYDROGEN BOND; MUTATION; OXIDATION; PSEUDOMONAS AERUGINOSA; STEREOCHEMISTRY;

ALANINE; BINDING SITES; HEME OXYGENASE (DECYCLIZING); HYDROGEN BONDING; LYSINE; MODELS, MOLECULAR; PSEUDOMONAS AERUGINOSA; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 1842688373     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja031791i     Document Type: Article

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18. The present results suggest two possibilities as functions of Lys34 and Lys132 in PigA. One is that both Lys34 and Lys132 interact with the heme propionate to hold the heme at the rotated position and the other is that either Lys34 or Lys132 interacts with the heme propionate and the other stabilizes the interaction. In the latter case, the mutation of the lysine stabilizing the interaction would destabilize the interaction, leading to partial break of the interaction. On the other hand, the mutation of the lysine interacting with the heme propionate would break the interaction, but partially form a new interaction between the other lysine and the heme propionate.