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Issue 18, 2009
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The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O2 and CO binding to iron protoporphyrin IX

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Abstract

Complexation of iron(II) protoporphyrin IX (Fe2+PP) into a genetically engineered heme pocket on recombinant human serum albumin (rHSA) creates an artificial hemoprotein which can bind O2 reversibly at room temperature. Here we highlight a crucial role of a basic amino acid triad the entrance of the heme pocket in rHSA (Arg-114, His-146, Lys-190) for O2 and CO binding to the prosthetic Fe2+PP group. Replacing His-146 and/or Lys-190 with Arg resolved the structured heterogeneity of the possible two complexing modes of the porphyrin and afforded a single O2 and CO binding affinity. Resonance Raman spectra show only one geometry of the axial His coordination to the central ferrous ion of the Fe2+PP.

Graphical abstract: The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O2 and CO binding to iron protoporphyrin IX

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Publication details

The article was received on 19 May 2009, accepted on 29 Jun 2009 and first published on 22 Jul 2009


Article type: Paper
DOI: 10.1039/B909794E
Citation: Org. Biomol. Chem., 2009,7, 3836-3841
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    The role of an amino acid triad at the entrance of the heme pocket in human serum albumin for O2 and CO binding to iron protoporphyrin IX

    T. Komatsu, A. Nakagawa, S. Curry, E. Tsuchida, K. Murata, N. Nakamura and H. Ohno, Org. Biomol. Chem., 2009, 7, 3836
    DOI: 10.1039/B909794E

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