Sugishima M., Kusumoto T., Sato H., Sakamoto H., Higashimoto Y., Yamamoto K., Taira J. "Heme regulatory motif of heme oxygenase-2 is involved in the interaction with NADPH-cytochrome P450 reductase and regulates enzymatic activity" (2025) Int. J. Mol. Sci. Special Issue "Intracellular Trafficking and Catabolism of Free Heme: Physiological Roles and Relevance to Pathological Mechanisms", 26, 2318. DOI: 10.3390/ijms26052318
Wada K., Kobayashi K., Era I., Isobe Y., Kamimura T., Marukawa M., Nagae T., Honjo K., Kaseda N., Motoyama Y., Inoue K., Sugishima M., Kusaka K., Yano N., Fukuyama K., Mishima M., Kitagawa Y., Unno M. "Protonation/deprotonation-driven switch for the redox stability of low-potential [4Fe-4S] ferredoxin" (2024) eLife, 13, RP102506. DOI: 10.7554/eLife.102506.2
Joutsuka T., Nanasawa R., Igarashi K., Horie K., Sugishima M., Hagiwara Y., Wada K., Fukuyama K., Yano N., Mori S., Ostermann A., Kusaka K., Unno M. "Neutron crystallography and quantum chemical analysis of bilin reductase PcyA mutants reveal substrate and catalytic residue protonation states" (2023) J. Biol. Chem., 299, 102763. DOI: 10.1016/j.jbc.2022.102763
Sato H., Sugishima M., Tsukaguchi M., Masuko T., Iijima M., Takano M., Omata Y., Hirabayashi K., Wada K., Hisaeda Y., Yamamoto K. "Crystal structures of hydroxymethylbilane synthase complexed with a substrate analog: a single substrate-binding site for four consecutive condensation steps" (2021) Biochem. J. 478, 1023-1042. DOI: 10.1042/BCJ20200996
Sugishima M., Taira J., Sagara T., Nakao R., Sato H., Noguchi M., Fukuyama K., Yamamoto K., Yasunaga T., Sakamoto H. "Conformational Equilibrium of NADPH–cytochrome P450 Oxidoreductase is Essential for Heme Oxygenase Reaction" (2020) Antioxidants Special Issue "Pharmacological and Clinical Significance of Heme Oxygenase-1", 9, 673. DOI: 10.3390/antiox9080673
Miyake K., Fushimi K., Kashimoto T., Maeda K., Win N., Kimura H., Sugishima M., Ikeuchi M., Narikawa R. "Functional diversification of two bilin reductases for light perception and harvesting in unique cyanobacterium Acaryochloris marina MBIC 11017" (2020) FEBS J. 287, 4016-4031. DOI: 10.1111/febs.15230
Sugishima M., Wada K., Fukuyama K., Yamamoto K. "Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome" (2020) J. Biol. Chem. 295, 771-782. DOI: 10.1016/S0021-9258(17)49934-0
Iijima M., Ohnuki J., Sato T., Sugishima M., Takano M. "Coupling of Redox and Structural States in Cytochrome P450 Reductase Studied by Molecular Dynamics Simulation" (2019) Sci. Rep. 9341. DOI: 10.1038/s41598-019-45690-2
Sugishima M., Sato H., Wada K., Yamamoto K. "Crystal structure of a NADPH-cytochrome P450 oxidoreductase(CYPOR) and heme oxygenase 1 fusion protein implies a conformation change in CYPOR upon NADPH/NADP+ binding" (2019) FEBS Lett., 593, 868-875. DOI: 10.1002/1873-3468.13360.
Igarashi K., Hagiwara Y., Sugishima M., Wada K., Fukuyama K., Ikeda A., Yano N., Kusaka K., Ostermann A., Unno M. "Crystal Growth of a Bilin Reductase PcyA I86D Mutant-Substrate Complex for Neutron Crystallography" (2018) Crystal Growth & Design 18, 5174-5181. DOI: 10.1021/acs.cgd.8b00607.
Takao H., Hirabayashi K., Nishigaya Y., Kouriki H., Nakaniwa T., Hagiwara Y., Harada J., Sato H., Yamazaki T., Sakakibara Y., Suiko M., Asada Y., Takahashi Y., Yamamoto K., Fukuyama K., Sugishima M., Wada K. "A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity" (2017) Nat. Commun. 8, 14397. DOI: 10.1038/ncomms14397
Hagiwara Y., Wada K., Irikawa T., Sato H., Unno M., Yamamoto K., Fukuyama K., Sugishima M. "Atomic-resolution structure of the phycocyanobilin:ferredoxin oxidoreductase I86D mutant in complex with fully protonated biliverdin" (2016) FEBS Lett. 590, 3425-3434.
Maeki M., Yamazaki S., Pawate S.A., Ishida A., Tani H., Yamashita K., Sugishima M., Watanabe K., Tokeshi M., Kenis P.J.A., Miyazaki M. "A microfluidic-based protein crystallization method in 10 micrometer-sized crystallization space" (2016) CrystEngComm 18, 7722-7727.
Unno M., Ishikawa-Suto K., Kusaka K., Tamada T., Hagiwara Y., Sugishima M., Wada K., Yamada T., Tomoyori K., Hosoya T., Tanaka I., Niimura N., Kuroki R., Inaka K., Ishihara M., Fukuyama K. "Insights into the proton transfer mechanism of a bilin reductase PcyA following neutron crystallography" (2015) J. Am. Chem. Soc. 137, 5452-5460.
Harada E., Sugishima M., Harada J., Fukuyama K., Sugase K. "Distal regulation of heme binding of heme oxygenase-1 mediated by conformational fluctuations" (2015) Biochemistry 54, 340-348.
Harada E., Sugishima M., Harada J., Noguchi M., Fukuyama K., Sugase K. "Backbone assignments of the apo and Zn(II) protoporphyrin IX-bound states of the soluble form of rat heme oxygenase-1" (2015) Biomol. NMR Assign. 9, 197-200
Sugishima M., Sato H., Higashimoto Y., Harada J., Wada K., Fukuyama K., Noguchi M. "Structural basis for the electron transfer from an open form of NADPH-cytochrome P450 oxidoreductase to heme oxygenase." (2014) Proc. Natl. Acad. Sci. USA 111, 2524-2529.
Sugishima M., Moffat K., Noguchi M. "Discrimination between CO and O2 in heme oxygenase: Comparison of static structures and dynamic conformation changes following CO photolysis." (2012) Biochemistry 51, 8554-8562.
Pattanayak, G. K., Venkataramani, S., Hörtensteiner, S., Kunz, L., Christ, B., Moulin, M., Smith, A. G., Okamoto, Y., Tamiaki, H., Sugishima, M., Greenberg, J. T. “ACCELERATED CELL DEATH2 in Mitochondria Modulates Cell Death and Suppresses Mitochondrial Oxidative Bursts in Arabidopsis.” (2012) Plant J. 69, 589-600.
Taira J., Sugishima M., Kida Y., Oda E., Noguchi M., Higashimoto Y. "Competitive inhibitor of heme oxygenase-1 (HO-1) with heme: identification of a minimum sequence in caveolin-1 for binding to HO-1." (2011) Biochemistry 50, 6824-6831.
Yamaoka M., Sugishima M., Noguchi M., Fukuyama K. Mizutani Y. “Protein dynamics of heme–heme oxygenase-1 complex following carbon monoxide dissociation.” (2011) J. Raman Spectrosc. 42, 910-916.
Watanabe A., Hirata K., Hagiwara Y., Yutani Y., Sugishima M., Yamamoto M., Fukuyama K., Wada K. “Expression, purification and preliminary X-ray crystallographic analysis of the cyanobacterial biliverdin reductase.” (2011) Acta Crystallogra. F67, 313-317.
Sato H., Higashimoto Y. Sakamoto H., Sugishima M., Shimokawa C., Harada J., Palmer G., Noguchi M. “Reduction of oxaporphyrin ring of CO-bound α-verdoheme complexed with heme oxygenase-1 by NADPH-cytochrome P450 reductase.” (2011) J. Inorg. Biochem. 105, 289-296.
Sugishima M., Okamoto Y., Noguchi M., Kohchi T., Tamiaki H., Fukuyama K. “Crystal structures of the substrate-bound forms of red chlorophyll catabolite reductase: implications for site-specific and stereospecific reaction.” (2010) J. Mol. Biol. 402, 879-891.
Hagiwara Y., Sugishima M., Khawn H., Kinoshita H., Inomata K., Shang L., Lagarias J. C., Takahashi Y., Fukuyama K. “Structural insights into vinyl reduction regiospecificity of phycocyanobilin:ferredoxin oxidoreductase (PcyA).” (2010) J. Biol. Chem. 285, 1000-1007.
Sugishima M., Kitamori Y., Noguchi M., Kohchi T., Fukuyama K. "Crystal structure of red chlorophyll catabolite reductase: enlargement of the ferredoxin-dependent bilin reductase family." (2009) J. Mol. Biol. 389, 376-387.
Takahashi K., Harada S., Higashimoto Y., Shimokawa C., Sato H, Sugishima M., Kaida Y., Noguchi M. "Involvement of metals in enzymatic and nonenzymatic decomposition of C-terminal alpha-hydroxyglycine to amide: an implication for the catalytic role of enzyme-bound zinc in the peptidylamidoglycolate lyase reaction." (2009) Biochemistry 48,1654-1662.
Sato H., Sugishima M., Sakamoto H., Higashimoto Y., Shimokawa C., Fukuyama K., Palmer G., Noguchi M. "Crystal structure of rat haem oxygenase-1 in complex with ferrous verdohaem: presence of a hydrogen-bond network on the distal side." (2009) Biochem. J. 419, 339-345.
Higashimoto Y., Sugishima M., Sato H., Sakamoto H., Fukuyama K., Palmer G., Noguchi M. "Mass spectrometric identification of lysine residues of heme oxygenase-1 that are involved in its interaction with NADPH-cytochrome P450 reductase." (2008) Biochem. Biophys. Res. Commun. 367, 852-858.
Sato H., Higashimoto Y., Sakamoto H., Sugishima M., Takahashi K., Palmer G., Noguchi M. "Electrochemical reduction of ferrous α-verdoheme in complex with heme oxygenase-1." (2007) J. Inorg. Biochem. 101, 1394-1399.
Sugishima M., Oda K., Ogura T., Sakamoto H., Noguchi M., Fukuyama K. "Alternative cyanide-binding modes to the haem iron in haem oxygenase." (2007) Acta Crystallogr. F63, 471-474.
Sugishima M., Higashimoto Y., Oishi, T., Takahashi H., Sakamoto H., Noguchi M., Fukuyama K. "X-ray crystallographic and biochemical characterization of the inhibitory action of an imidazole-dioxolane compound on heme oxygenase." (2007) Biochemistry 46, 1860-1867.
Hagiwara Y., Sugishima M., Takahashi Y., Fukuyama K. "Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form." (2006) FEBS Lett. 580, 3823-3838.
Hagiwara Y., Sugishima M., Takahashi Y., Fukuyama K. "Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phycocyanobilin." (2006) Proc. Natl. Acad. Sci. USA 103, 27-32.
Sugishima M., Hagiwara Y., Zhang X., Yoshida T., Migita C. T., Fukuyama K. "Crystal structure of dimeric heme oxygenase-2 from Synechocystis sp. PCC 6803 in complex with heme." (2005) Biochemistry 44, 4257-4266.
Higashimoto Y., Sakamoto H., Hayashi S., Sugishima M., Fukuyama K., Palmer G., Noguchi M. "Involvement of NADPH in the interaction between heme oxygenase-1 and cytochrome P450 reductase." (2005) J. Biol. Chem. 280, 729-737.
Sugishima M., Tanimoto N., Soda K., Hamada N., Tokunaga F., Fukuyama K. "Structure of photoactive yellow protein (PYP) E46Q mutant at 1.2 Å resolution suggests how Glu46 controls the spectroscopic and kinetic characteristics of PYP." (2004) Acta Crystallogr. D60, 2305-2309.
Sugishima M., Migita C. T., Zhang X., Yoshida T., Fukuyama K. "Crystal structure of heme oxygenase-1 from cyanobacterium Synechocystis sp. PCC 6803 in complex with heme." (2004) Eur. J. Biochem. 271, 4517-4525.
Sugishima M., Sakamoto H., Noguchi M., Fukuyama K. "CO-trapping site in heme oxygenase revealed by photolysis of its CO-bound heme complex: mechanism of escaping from product inhibition." (2004) J. Mol. Biol. 341, 7-13.
Sakamoto H., Higashimoto Y., Hayashi S., Sugishima M., Fukuyama K., Palmer G., Noguchi M. "Hydroxylamine and hydrazine bind directly to the heme iron of the heme-heme oxygenase-1 complex." (2004) J. Inorg. Biochem. 98, 1223-1228.
Taguchi Y., Sugishima M., Fukuyama K. "Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8." (2004) Biochemistry 43, 4111-4118.
Sugishima M., Sakamoto H., Noguchi M., Fukuyama K. "Crystal structures of ferrous and CO-, CN--, and NO-bound forms of rat heme oxygenase-1 (HO-1) in complex with heme: Structural implications for discrimination between CO and O2 in HO-1." (2003) Biochemistry 42, 9898-9905.
Sugishima M., Sakamoto H., Higashimoto Y., Noguchi M., Fukuyama K. "Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate: Conformational change of the distal helix during the heme cleavage reaction." (2003) J. Biol. Chem. 278, 32352-32358.
Sugishima M., Sakamoto H., Higashimoto Y., Omata Y., Hayashi S., Noguchi M., Fukuyama K. "Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide: Implication for regiospecific hydroxylation of heme at the α-meso carbon." (2002) J. Biol. Chem. 277, 45086-45090.
Sugishima M., Sakamoto H., Kakuta Y., Omata Y., Hayashi S., Noguchi M., Fukuyama K. "Crystal structure of rat apo-heme oxygenase-1 (HO-1): Mechanism of heme binding in HO-1 inferred from structural comparison of the apo and heme complex forms." (2002) Biochemistry 41, 7293-7300.
Sugishima M., Omata Y., Kakuta Y., Sakamoto H., Noguchi M., Fukuyama K. "Crystal structure of rat heme oxygenase-1 in complex with heme." (2000) FEBS Lett. 471, 61-66.
杉島正一 ”誘導型ヘム分解酵素HO-1の酸化還元複合体構造” (2025) 月刊「細胞」, 57 (9), 68-71. (出版社の依頼によるBio Clinicaからの転載）
杉島正一 ”ポルフィリン代謝酵素群の構造研究” (2025) 日本結晶学会誌, 67(2), 80-87. DOI: 10.5940/jcrsj.67.80
杉島正一 ”誘導型ヘム分解酵素HO-1の酸化還元複合体構造” (2025) BIO Clinica, 40 (3), 49-53.
Unno M., Joutsuka T., Sugishima M., Wada K., Hagiwara Y., Yano N., Kusaka K., Ostermann A. " Neutron crystallography combined with QM/MM calculations of bilin reductase PcyA mutants reveal substrate and catalytic residue protonation states" (2024) Joint Annual Report 2023 of the MLZ and FRM II, 36.
海野昌喜、城塚達也、杉島正一、和田啓、萩原義徳、矢野直峰、Andreas Ostermann、日下勝弘 "ビリン還元酵素PcyAの二つの変異体の吸収スペクトル及び反応の変化とプロトン化状態の相関" （2023）日本中性子科学会誌「波紋」, 33, 151-156.
Sugishima M., Wada K., Fukuyama K. "Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures" (2020) Curr. Med. Chem., 27, 3499-3518. DOI: 10.2174/0929867326666181217142715
Sugishima M., Wada K., Unno M., Fukuyama K. "Bilin-metabolizing enzymes: site-specific reductions catalyzed by two different type of enzymes" (2019) Curr. Opin. Struct. Biol., 59, 73-80. DOI: 10.1016/j.sbi.2019.03.005
海野昌喜、日下勝弘、玉田太郎、杉島正一、和田啓、萩原義徳、福山恵一 "ビリン還元酵素PcyAと基質ビリベルジン複合体の中性構造解析から見えてきたもの" （2016）日本中性子科学会誌「波紋」, 26,130-134.
Unno M., Ishikawa-Suto K., Kusaka K., Tamada T., Hagiwara Y., Sugishima M., Wada K., Ishikawa M., Fukuyama K. "Neutron Crystallography Reveals Two Protonation States of PcyA, a Bilin Reductase" (2016) MLF Annual Reports 2014, 15-17.
杉島正一 "ヘム代謝系関連酵素の構造生物学的研究" （2016） 生化学、88、171-181.
杉島正一 "X線小角散乱によるNADPH-シトクロムP450還元酵素とヘムオキシゲナーゼの複合体の構造解析" （2016）九州シンクロトロン光研究センター年報2014、14-16.
福山恵一、和田啓、杉島正一、海野昌喜 "光合成色素フィコシアノビリンを合成する酵素と基質ビリベルジンとの複合体の中性子結晶解析" （2015） 生化学、87、753-757.
海野昌喜、杉島正一、和田啓、萩原義徳、日下勝弘、玉田太郎、福山恵一 "中性子結晶構造解析で明らかになったビリン還元酵素PcyA基質複合体の二つの水素化状態と構造的特徴" (2015) 日本結晶学会誌、57, 297-303.
Sugishima M., Fukuyama K., Noguchi M. "Crystal structure of an associated form of NADPH-cytochrome P450 reductase with heme oxygenase" (2015) SPring-8 Research Frontiers 2014, 18-19.
杉島正一 "ヘム鉄代謝の鍵となる電子伝達複合体の構造解析" (2014) 日本結晶学会誌, 56, 393-398.
杉島正一 "ヘムオキシゲナーゼの立体構造と機能" (2013) 久留米醫學會雑誌 76, 249-254.
杉島正一 "ヘムの代謝にかかわる酵素の構造生物学" (2007) 日本結晶学会誌 49, 99-106.
杉島正一、萩原義徳、高橋康弘、福山恵一 "フェレドキシン依存性ビリン還元酵素の構造研究" (2006) 日本結晶学会誌 48, 283-289.
Fukuyama K., Sugishima M. "Structure of phycobilin synthesis enzyme." (2006) SPring-8 Research Frontiers 2005, 22-23.
坂本寛、杉島正一、東元祐一郎、福山恵一、野口正人 "ヘムオキシゲナーゼの構造と機能" (2005) 生化学 77, 634-638.
Sakamoto H., Sugishima M., Omata Y., Kakuta Y., Fukuyama K., Palmer G., Noguchi M. "Structure and reaction mechanism of heme oxygenase-1." (2002) International Congress Series 1233, 183-189.
Sugishima M., Wada K., Taira J. "Proteins Associated with Haem Catabolism for Iron Utilisation and Other Functions in Mammals and Photosynthetic Organisms." in Iron in Biology - Molecular Structures, Cellular Processes and Living Systems, Shiro Y., Sawai H., Tosha T. eds. (2025) RSC publishing, 121-137. DOI: 10.1039/9781837677979
杉島正一 ”フェレドキシン依存性酸化還元酵素の構造と機能”, 日本の結晶学（II)－その輝かしい発展－ (2014) 日本結晶学会、294.
Unno M., Sugishima M., Wada K., Fukuyama K. "Structure-function relationships of ferredoxin-dependent bilin reductases." in Integrating approach of photofunctional hybrid materials for energy and envirionment, Akitsu T. eds. (2013) Nova Science Publishers, 47-68.
福山恵一、杉島正一 "生体高分子の形と機能", 基礎医学・生物系の同位体実験－放射性同位体・安定同位体・Ｘ線結晶解析の基礎－ (2005) 久留米大学、99-113.
杉島正一 ”ポルフィリン代謝酵素群の構造生物研究” (2024) 令和6年度日本結晶学会年会, 名古屋（日本結晶学会賞・学術賞受賞講演）
杉島正一 ”ヘム分解酵素と還元酵素の相互作用に関する構造生物学的研究” (2024) 令和6年度日本生化学会大会公募シンポジウム「テトラピロール色素が織りなす多彩な機能とその生合成」, 横浜
Sugishima M. "Structural analysis of NADPH-cytochrome P450 reductase in complex with heme oxygenase reveals how reductase supplies reducing equivalents to mono-oxygenase" (2023) 日本薬物動態学会第38回年会・第23回シトクロムP450国際会議国際合同大会, 静岡
杉島正一 "ヘム分解酵素HO-1における COとO2の厳密な識別機構" (2019) 第 92 回日本生化学会大会公募シンポジウム「テトラピロール色素が織りなす多様な機能とその生合成系の最前線」, 横浜
杉島正一 "ヘム代謝系関連酵素の構造生物学的研究" （2015）第38回日本分子生物学会年会・第88回日本生化学会大会合同大会、神戸（日本生化学会奨励賞受賞講演）
杉島正一 ”打撲後のあざの色調変化に隠されたメカニズム ～ヘム分解酵素の立体構造と反応機構～” (2015) 九州大学先導物質化学研究所・九州シンクロトロン光研究センター合同シンポジウム - 物質化学が導く材料創生とシンクロトロン放射光が解く構造・機能のコラボレーション -、鳥栖（科学技術分野の文部科学大臣表彰 若手科学者賞受賞記念講演）
杉島正一 ”シトクロムP450還元酵素の大きな構造変化を伴うヘムオキシゲナーゼへの電子伝達機構” （2015） 大阪大学蛋白質研究所セミナー「生体超分子構造解析ビームライン利用報告会」、吹田
杉島正一 ”赤血球が壊れた後、ヘモグロビンはどのように代謝されるのか？- ヘム分解酵素（ヘムオキシゲナーゼ）の立体構造と反応機構 -” (2015) 宮崎大学テニュアトラック推進機構主催セミナー 「蛋白質立体構造解析の最前線」、宮崎
杉島正一 "ヘム分解酵素ヘムオキシゲナーゼの立体構造と機能" (2014) 第 87 回日本生化学会大会公募フォーラム「ヘム・ビリン代謝の生化学と構造生物学」, 京都
Sugishima M. “Structural basis for the electron transfer from NADPH-cytochrome P450 reductase to mammalian heme oxygenase-1” (2014) 8th International Conference on Heme Oxygenases, BioIron & Oxidative Stress, Sydney, Australia.
杉島正一 "ヘムオキシゲナーゼ(HO)の立体構造変化と機能" (2014) 九州大学先導物質化学研究所講演会, 福岡
杉島正一 "ヘムオキシゲナーゼによるCOとO2の識別機構に.関する構造生物学的研究" (2013) 平成25年度日本生化学会九州支部例会、佐賀（日本生化学会九州支部学術奨励賞受賞講演）
Sugishima M. “Structural insights into ferredoxin dependent bilin reductases” (2010) AsCA2010, Busan, Korea.
Sugishima M. "How phycobilins are synthesized from heme ? - View from the crystal structure -" (2007) International Symposium on Biosynthesis of Tetrapyrroles, Kusatsu, Japan.
杉島正一、坂本寛、東元祐一郎、大石徹、高橋秀典、野口正人、福山恵一 "ラット由来ヘムオキシゲナーゼ－１を用いた構造生物学的研究" (2007) 分子研研究会 「ヘム代謝に関わる酵素の分子科学」、岡崎
Sugishima M. "Structural basis for heme degradation by heme oxygenase." (2006) AsCA'06/CrSJ, Tsukuba, Japan.（日本結晶学会賞・進歩賞受賞講演）
杉島正一 "ヘムの代謝に関わる酵素の構造生物学的研究" (2006) 21世紀COEプログラム拠点「細胞超分子装置作動原理の解明と再構成」研究発表会「21世紀 COE から未来への架け橋」、千里ライフサイエンスセンター、豊中
"タンパク質の立体構造から見えてくること ～打撲後のあざの色調変化に隠された分子メカニズムを例にとって～" 久留米工業高等専門学校 (2019)
"光合成生物におけるヘム代謝酵素のX線結晶解析" 九州工業大学 (2010)
" ヘム代謝酵素のX線結晶解析" 立命館大学大学院特殊講義「光と生命」 第100回生物有機化学・草津セミナー(2009)