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生体エネルギー変換における金属イオンと蛋白質の役割

Research Project

Project/Area Number 08249106
Research Category

Grant-in-Aid for Scientific Research on Priority Areas (A)

Allocation TypeSingle-year Grants
Research InstitutionOkazaki National Research Institutes

Principal Investigator

北川 禎三  岡崎国立共同研究機構, 分子科学研究所, 教授 (40029955)

Co-Investigator(Kenkyū-buntansha) 堀 洋  大阪大学, 理学部, 助手 (20127294)
成田 吉徳  九州大学, 有機化学基礎研究センター, 教授 (00108979)
吉川 信也  姫路工業大学, 理学部, 教授 (40068119)
茂木 立志  東京大学, 大学院・理学系研究科, 助手 (90219965)
高妻 孝光  茨城大学, 理学部, 助教授 (50215183)
柏木 浩  九州工業大学, 情報工学部, 教授 (10000853)
Project Period (FY) 1996 – 1999
Project Status Completed (Fiscal Year 1999)
Budget Amount *help
¥161,200,000 (Direct Cost: ¥161,200,000)
Fiscal Year 1999: ¥27,200,000 (Direct Cost: ¥27,200,000)
Fiscal Year 1998: ¥49,400,000 (Direct Cost: ¥49,400,000)
Fiscal Year 1997: ¥51,700,000 (Direct Cost: ¥51,700,000)
Fiscal Year 1996: ¥32,900,000 (Direct Cost: ¥32,900,000)
Keywords末端酸化酵素 / 光合成 / プロトンポンプ / 電子伝達 / 呼吸鎖 / チトクロム酸化酵素 / 銅タンパク質 / 振動スペクトル / 生体エネルギー変換 / 金属タンパク質 / 共鳴ラマン / 光合成反応中心タンパク複合体 / プロトン輸送
Research Abstract

本班は生体エネルギー変換のうちで最も基本的な呼吸鎖及び光合成電子伝達系の金属タンパクを取り扱う研究者とタンパク中の電子伝達やプロトン輸送という現象を中心に調べる研究者、その他蛋白高次構造とか磁性に注目する研究者が、共同研究の課題をたてて、特定領域研究グループとしての特徴を発揮するように努力した。
酸素呼吸をする生物は、栄養素の代謝で得られる電子を電子伝達系という蛋白群を通して酸素分子に伝達し、その電子移動で駆動されるプロトンポンプを動かして、H^+濃度勾配をつくる。ウシの末端酸化酵素の3次元構造が本班の班員により解明され、国際的な注目を浴びた。本年はその分解能が2.3Åまで進んだ。その反応機構に関しても時間分解振動分光の実験が進み、酸素が水になる程度の全部の中間体が検出されると共に、プロトン輸送に関する赤外吸収の研究も進んだ。錯体科学的にこの鉄-銅2核活性部位を合成する事にも成功し、そこに結合した酸素の振動スペクトルも得られた。哺乳類の末端酸化酵素はチトクロムaa_3型であるが大腸菌のそれはチトクロムbo_3型でその分子生物学的研究により鉄-銅2核活性部位の重要アミノ酸残基の役割に関する研究が進んだ。またaa_3型とbo_3型のキメラ蛋白も作られて生物進化に関する解析もなされた。bo_3型酵素もaa_3型と同じ反応機構で進むと考えられるが、そのP中間体に対しチロシンラジカルのシグナルが検出され国際的な注目を浴びている。

Report

(4 results)
  • 1999 Annual Research Report
  • 1998 Annual Research Report
  • 1997 Annual Research Report
  • 1996 Annual Research Report
  • Research Products

    (24 results)

All Other

All Publications (24 results)

  • [Publications] T. tomita et al.: "Resonance Raman investigation of Fe-N-O structure of nitrosylheme in myoglobin and its mutants"Journal of Physical Chemistry Part B. 103. 7044-7054 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] T. Iwase et al.: "Infrared evidence for Cu_B ligation of photodissoclated CO of cytochrome c oxidase at ambient temperatures and accompanied deprotonation of a carboxyl side chain of protein"Journal of American Chemical Society. 121. 1415-1416 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] Y. Yoshikawa et al.: "Redox-coupled crystal structural changesin bovine heart cytochrome c oxidase"Science. 280. 1723-1729 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] F. Tani et al.: "Synthesis of Heme-tris(imidazoyl)methane Copper Complex, the First Binuclear Complex Bearing Three Inidazole Ligands for copper, as an Active Site Model of Cytochrome c Oxidase"Royal Chemical Society: Chemical Communication. 36. 1731-1732 (1998)

    • Related Report
      1999 Annual Research Report
  • [Publications] H. Shimada et al.: "Putidaredooxin-Cytochrome P450cam Interaction: Spin State of the Heme Iron Modulates Putidaredooxin Strurcture"Journal of Biological Chemistry. 274. 9363-9369 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] T. Mogi et al.: "Role of a bound ubiquinone on reactions of the Escherichia coil cytochrome bo with ubiquinol oxidase"FEBS Letters. 457. 61-64 (1999)

    • Related Report
      1999 Annual Research Report
  • [Publications] Mizutani,Y.et al.: "Direct obervation of cooling of heme upon photo-dissociation of carbonmonoxy myogiobin Progress in Inorganic Chemistry" Science. 278. 443-446 (1997)

    • Related Report
      1998 Annual Research Report
  • [Publications] S.Yoshikawa et.al.: "Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase" Science. 280. 1723-1729 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] R.Tani et al.: "Synthesis of Heme-tris(imidazoyl)methane copper complex,the first binuclear complex bearing three imidazole ligands for copper,as an active site model of cytochrome c oxidase" J.Chem.Soc.Chem.Commun.1731-1732 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] M.Tsubaki et al.: "Resonance Raman,Infrared and EPR investigation on the binuclear site structure of the heme-copper ubiquinol oxidases from Acetobacter aceti Effect of the heme peripheral formyl group substitution" Biochemistry. 36. 13034-13042 (1997)

    • Related Report
      1998 Annual Research Report
  • [Publications] Mogi,T. et al.: "Ubstitutions of conserved aromatic amino acid residues in subunit I perturb the metal centers of the Escherichia coli bo-type Ubiquinol oxidase." Biochemistry. 272. 1632-1639 (1998)

    • Related Report
      1998 Annual Research Report
  • [Publications] F.Sato et al.: "Development of A New Density Functional Program for All Electron Calculation of Proteins" Int.J.Quant.Chem.63. 245-256 (1997)

    • Related Report
      1998 Annual Research Report
  • [Publications] T.Kitagawa, et al.: "Oxygen Activation Mechanism at Binuclear Site of Heme-Copper Oxidase Superfamily Revealed by Time-Resolved Resonance Raman Spectroscopy" Progress in Inorganic Chemistry. 45. 431-479 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] X.Zhao, et al.: "Observation of the Resonance Raman Spectra of the Semiquinones. Q_A and Q_B in Photosynthetic Reaction Centers from Rb.Sphaeroides R26" Journal of the American Chemical Society. 119. 5263-5264 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] T.Tsukihara, et al.: "The Whole Structure of the 13 Subunit Oxidized Bovine Heart Cytochrome c Oxidase at 2.8Å" Science. 272. 1136-1144 (1996)

    • Related Report
      1997 Annual Research Report
  • [Publications] F.Sato, et al.: "Development of a New Density Functional Program for All Electrons Calculation of Proteins" International Journal of Quantum Chemistry. 63. 245-256 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] M.Tsubaki, et al.: "Existence of Two Heme B Centers in Cytochrome b561 from Bovine Adrenal Chromaffin Vesicles as Revealed by a New Purification Procedure and EPR Spectroscopy" Journal of Biological Chemistry. 272. 23206-23210 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] K.Saiki, et al.: "Exploring Subunit-Subunit Interactions in the Escherichia coli bo-type Ubiquinol Oxidase by Extragenic Suppressor Mutation Analysis" Journal of Biological Chemistry. 272. 14721-14726 (1997)

    • Related Report
      1997 Annual Research Report
  • [Publications] T.Ogura et al.: "Time-Resolved Resonance Raman Evidence for Tight Coupling between Electron Transfer and Proton Pumping of Cytochrome c Oxidase upon the Chenge from the Fev Oxidation Level to the Fe^<IV> Oxidation Level" Journal of the American Chemical Society. 118. 5443-5449 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] D.A.Proshlyakov et al.: "Resonance Raman/absorption characterization of the oxo-intermediates of cytochrome c oxidase generated in its reaction with hydrogen peroxide : pH and H_2O_2 concentration dependence" Biochemistry. 35. 8580-8586 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] T.Tsukihara et al.: "The whole structure of the 13 subunit oxidized bovine heart cytochrome c oxidase at 2.8Å" Science. 272. 1136-1144 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] M.Tsubaki et al.: "FT-IR and EPR studies on cyanide-bindings to the heme-copper binuclear center of cytochrome bo-type ubiquinol oxidase from Escherichia coli : Release of Cu_B-cyano complex in the partially reduced states" Journal of Biological Chemistry. 271. 4017-4022 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] H.Hori et al.: "EPR and NO complex of bd-type ubiquinol oxidase from Escherichia coli. The proximal ligand of heme d is a nitrogenous amino acid residue" Journal of Biological Chemistry. 271. 9254-9258 (1996)

    • Related Report
      1996 Annual Research Report
  • [Publications] T.Sakuma et al.: "Ab initio MO Study of the Chlorophyll Dimer in the Photosynthetic Reaction Center. I.A Theoretical Treatment of the Electrostatic Field Created by Surrounding Proteins" International Journal of Quantum Chemistry. 61. 137-151 (1997)

    • Related Report
      1996 Annual Research Report

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Published: 1996-04-01   Modified: 2016-04-21  

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