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Structural study on higher plant type heme oxygenase-1

東田, 怜 大阪大学 DOI:10.18910/82034

2021.03.24

概要

ヘムオキシゲナーゼ（HO）はヘム代謝に関わる酵素であり、ヘムを鉄イオン、一酸化炭素、ビリベルジンに分解する。これまでの研究で、HOは多くの生物種に共通して保存されていることが確認されている。結晶構造が明らかにされている哺乳類型とシアノバクテリア型HOでは、それぞれ８または９本のα-ヘリックスで構成されたよく似た立体構造をとることが判っていた。基質であるヘムは、そのうち２本のα-ヘリックスで形成される“ヘムポケット”に配位し、構造既知の全てのHO間で酵素反応や立体構造の基本骨格が共通していると考察されている。

　しかし、HOのアミノ酸配列比較からは，高等植物のHOだけが特徴的なアミノ酸配列を持ち，哺乳類またシアノバクテリアに対してそれぞれ２０％台と配列の保存性が著しく低いことが指摘されていた。特に基質であるヘムの配位子でなるHis残基が高等植物ではLys残基に置換されていること、さらにプロトン供給に重要なAsp残基もHis残基に置換されていることなど、高等植物型HOはヘム周辺環境が他種HOと大きく異なっていると推察されていた。しかし、これまで高等植物型HOの立体構造は解析されていないため、その構造・機能相関について詳細な議論ができていなかった。また、ヘム分解反応時に必要な電子を供給する電子供与体との相互作用についても、哺乳類型では電子供与体CPRとの複合体構造が報告されている一方で、高等植物では電子供与体であるフェレドキシン （Fd）との相互作用様式は未解明のままであった。

　本研究では、ダイズ（Glycine max）由来HO（GmHO-1）の立体構造をX線結晶構造解析により決定し、他種HOとの構造比較を行うことで、高等植物型HOがもつユニークなヘムポケット周辺構造を明らかにすることを目指した。さらに、基質であるヘムと電子供与体であるFdとの相互作用の詳細を解明するため，ITCをはじめとする各種熱測定およびNMR測定を行うこととした。その結果、鉄の異常散乱を用いたSAD法により位相決定に成功し、最終的に 1.06Å分解能で構造決定を行った。今回得られたGmHO-1の構造と他種HOの結晶構造とを比較したところ、ヘムポケットを形成している２本のα-ヘリックスのうち、N末端側のα-ヘリックスの直後に不規則な新しい構造領域が存在することが確認された。また、この不規則な構造領域の挿入により、ヘムポケットの反対側に新しい分子内トンネルを確認することができた。高等植物では、日照条件によりストロマ内のpHが７から８に変化することが知られている。ヘム分解反応に必要なプロトンを確実に供給するための構造最適化が起こったと考えられる。さらに、ヘムポケット内の静電ポテンシャルを計算したところ、高等植物型HOではヘムポケットの一部が負に帯電していることがわかった。先行研究で、反応中間体であるベルドヘムが高等植物型HOでのみ安定に結合することが報告されており、この特徴は静電的なポケット内表面物性の違いによるものであると結論づけた。

　次に、GmHO-1が示すFdとの相互作用がヘム結合時と非結合時とで異なるのかを確認するため，二状態でITC測定を行った。その結果、ヘム依存的にFdと相互作用をしていることを確認すると同時に、GmHO-1とFdとの複合体形成はエントロピーによって駆動されることを明らかにした。さらに、残基レベルでの相互作用部位を特定するために NMR測定を行ったところ、Fdに含まれている鉄硫黄クラスター周辺残基とGmHO-1内のヘム周辺で複合体界面を構成することが確認された。得られたNMRの化学シフト摂動の結果をもとに、ドッキングシミュレーションソフト HADDOCKを用いて複合体構造の予測を行ったところ、FdはGmHO-1のヘムポケットに埋もれるような形で相互作用するモデルを提供することができた。この時、鉄硫黄クラスターとヘムの距離は約５Åであり、鉄硫黄クラスターからヘムへ直接電子伝達が行われると示唆される。

　以上、高等植物型HOの立体構造を初めて解明すると同時に、高等植物型に特有の生理機能に対応した構造基盤を導き出すことができた。さらに，ITCやNMRを用いてFdとの最も確からしい複合体モデルを構築することができ、高等植物型HOがもつ特徴的なアミノ酸配列の構造的意味について，その詳細なモデルを提案することができた。

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