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Structure and Ligand Binding Properties of Myoglobins Reconstituted with Monodepropionated Heme:  Functional Role of Each Heme Propionate Side Chain,

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    Structure and Ligand Binding Properties of Myoglobins Reconstituted with Monodepropionated Heme:  Functional Role of Each Heme Propionate Side Chain†,‡
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    Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita 565-0871, Japan, Graduate School of Life Science, University of Hyogo, Ako 678-1297, Japan, Department of Physical Chemistry and 21 Century COE Program, Kyoto Pharmaceutical University, Kyoto 607-8414, Japan, PRESTO, JST, Saitama 332-0012, Japan, Harima Institute, RIKEN SPring-8 Center, Sayo 679-5148, Japan, Department of Chemistry and Biochemistry, Graduate School of Engineering, Kyushu University, Fukuoka 819-0395, Japan, Institute for Molecular Science, Okazaki 444-8787, Japan
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    Biochemistry

    Cite this: Biochemistry 2007, 46, 33, 9406–9416
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    https://doi.org/10.1021/bi7007068
    Published July 18, 2007
    Copyright © 2007 American Chemical Society
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    Abstract

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    Two heme propionate side chains, which are attached at the 6 and 7 positions of the heme framework, are linked with Arg45 and Ser92, respectively, in sperm whale myoglobin. To evaluate the role of each propionate, two kinds of one-legged hemins, 6-depropionated and 7-depropionated protohemins, were prepared and inserted into the apomyoglobin to yield two reconstituted proteins. Structural data of the reconstituted myoglobins were obtained via an X-ray crystallographic analysis at a resolution of 1.1−1.4 Å and resonance Raman spectroscopy. It was found that the lack of the 6-propionate reduces the number of hydrogen bonds in the distal site and clearly changes the position of the Arg45 residue with the disrupting Arg45−Asp60 interaction. In contrast, the removal of the 7-propionate does not cause a significant structural change in the residues of the distal and proximal sites. However, the resonance Raman studies suggested that the coordination bond strength of the His93−Fe bond for the protein with the 7-depropionated protoheme slightly increases compared to that for the protein with the native heme. The O2 and CO ligand binding studies for the reconstituted proteins with the one-legged hemes provide an important insight into the functional role of each propionate. The lack of the 6-propionate accelerates the O2 dissociation by ca. 3-fold compared to those of the other reconstituted and native proteins. The lack of the 7-propionate enhances the CO affinity by 2-fold compared to that of the protein with the native heme. These results indicate that the 6-propionate clearly contributes to the stabilization of the bound O2, whereas the 7-propionate plays an important role in the regulation of the Fe−His bond.

    Copyright © 2007 American Chemical Society

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    †

     This study was supported by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology. K.H. thanks the Japan Society for the Promotion of Science (JSPS) for the financial support.

    ‡

     Refined coordinates and structure factors have been deposited in the Protein Data Bank (entries 2EKT and 2EKU for aquometmyoglobins reconstituted with 6-depropionated and 7-depropionated protohemin IX species, respectively).

    §

     Osaka University.

    ‖

     University of Hyogo.

    ⊥

     RIKEN SPring-8 Center.

    @

     Kyoto Pharmaceutical University.

    Δ

     JST.

    ◊

     Present address:  Graduate School of Materials Science, Nara Institute of Science and Technology, Ikoma 630-0192, Japan.

    +

     Kyushu University.

    *

     To whom correspondence should be addressed:  Department of Applied Chemistry, Osaka University, Suita 565-0871, Japan. Phone and fax:  +81-6-6879-7928. E-mail:  [email protected].

    #

     Institute for Molecular Science.

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    Biochemistry

    Cite this: Biochemistry 2007, 46, 33, 9406–9416
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bi7007068
    Published July 18, 2007
    Copyright © 2007 American Chemical Society
    Request reuse permissions

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