反応中間体構造から明らかになった電子伝達タンパク質間の酸化還元依存的な親和性調節機構  [in Japanese] Molecular Mechanism of the Redox-dependent Interaction between NADH-dependent Ferredoxin Reductase and Rieske-type Ferredoxin  [in Japanese]

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Author(s)

    • 木村 成伸 KIMURA Shigenobu
    • 茨城大学工学部生体分子機能工学科 Department of Biomolecular Functional Engineering, Faculty of Engineering, Ibaraki University
    • 千田 俊哉 SENDA Toshiya
    • 産業技術総合研究所 バイオメディシナル情報研究センター Biomedicinal Information Research Center (BIRC), National Institute of Advanced Industrial Science and Technology (AIST)

Abstract

Redox-dependent affinity regulation is critical to fast and efficient electron transfer (ET) between ET proteins. The molecular mechanism of the affinity regulation, however, remains elusive due to the lack of crystal structures of the ET proteins in every redox state relevant to the ET reaction. BphA4 and BphA3 are, respectively, an FAD-containing NADH-dependent ferredoxin reductase and a Rieske-type [2Fe-2S] ferredoxin of a biphenyl dioxygenase BphA derived from <I>Acidovorax</I> sp. strain KKS 102. Our biochemical study showed that the reduction of the FAD in BphA4 increases the affinity between BphA3 and BphA4 approximately 20-fold. In order to reveal the molecular mechanism of this redox-dependent affinity regulation, we determined the crystal structure of the following molecular species: BphA4 in oxidized, hydroquinone, semiquinone, and reoxidized forms; BphA3 in oxidized and reduced forms; and the ET complex of BphA3 and BphA4. A comparative analysis of these seven crystal structures obtained revealed that a series of conformational changes of BphA4 occurs upon reduction of FAD to form a high-affinity BphA3-binding site in BphA4.

Journal

  • Nihon Kessho Gakkaishi

    Nihon Kessho Gakkaishi 50(6), 341-347, 2009-01-20

    The Crystallographic Society of Japan

References:  19

Codes

  • NII Article ID (NAID)
    10023987813
  • NII NACSIS-CAT ID (NCID)
    AN00188364
  • Text Lang
    JPN
  • Article Type
    ART
  • ISSN
    03694585
  • NDL Article ID
    9779411
  • NDL Source Classification
    ZM46(科学技術--地球科学--岩石・鉱物・鉱床)
  • NDL Call No.
    Z15-138
  • Data Source
    CJP  NDL  J-STAGE 
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