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114. CO complex of Myoglobin Mb-YQR at 100K

Author

Brunori, M., primary, Vallone, B., additional, Cutruzzola, F., additional, Travaglini-Allocatelli, C., additional, Berendzen, J., additional, Chu, K., additional, Sweet, R.M., additional, and Schlichting, I., additional

Published
2000
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129. Contributory presentations/posters

Author

Manoj, N., Srinivas, V., Surolia, A., Vijayan, M., Suguna, K., Ravishankar, R., Suguna, K., Surolia, A., Vijayan, M., Schwarzenbacher, R., Zeth, K., Diederichs, Kostner, G., Gries, A., Laggner, P., Prassl, R., Madhusudan, Akamine, Pearl, Xuong, Nguyen-huu, Taylor, Susan, Sagar, M., Ravishankar, R., Saikrishnan, K., Roy, S., Purnapatre, K., Handa, P., Varshney, U., Vijayan, M., Biswal, B., Sukumar, N., Vijayan, M., Rao, J., Johnson, A., Pattabhi, Vasantha, Krishna, S., Sastri, Mira, Savithri, H., Murthy, M., Pillai, Bindu, Kannan, Hosur, M., Kumar, Mukesh, Patwardhan, Swati, Kannan, K., Hosur, M., Padmanabhaa, B., Sasaki-Sugio, S., Nukaga, M., Matsuzaki, T., Karthikevan, S., Sharma, S., Sharma, A., Paramasivam, M., Kumar, P., Khan, J., Yadav, S., Srinivasan, A., Singh, T., Gourinath, S., Alam, Neelima, Srintvasan, A., Singh, T., Chandra, Vikas, Kaur, Punit, Betzel, Ch., Singh, T., Ghosh, S., Bera, A., Bhattacharya, S., Chakraborty, S., Pal, A., Mukhopadhyay, B., Dey, I., Haldar, U., Baneriee, Asok, Sevcik, Jozef, Solovicova, Adriana, Sekar, K., Sundaralingam, M., Betzel, Ch., Genov, N., Singh, T., Liang, Dong-cai, Jiang, Tao, Zhang, Ji-ping, Chang, Wen-rui, Jahnke, Wolfgang, Blommers, Marcel, Panchal, S., Hosur, R., Pillay, Bindu, Hosur, M., Mathur, Puniti, Srivatsun, S., Joshi, Ratan, Jaganathan, N., Chauhan, V., Atreya, H., Sahu, S., Chary, K., Govil, Girjesh, Adjadj, Elisabeth, Quinjou, Éric, Izadi-Pruneyre, Nadia, Blouquit, Yves, Mispelter, Joël, Heyd, Bernadette, Lerat, Guilhem, Milnard, Philippe, Desmadreil, Michel, Lin, Y., Rao, B., Raghunathan, Vidva, Chau, Mei, Rao, B., Pesais, Prashant, Srivastava, Sudha, Coutinho, Evans, Saran, Anil, Sapico, Leizl, Gesme, Jayson, Lijima, Herbert, Paxton, Raymond, Srikrishnan, Thamarapu, Grace, C., Nagenagowda, G., Lynn, A., Cowsik, Sudha, Sahu, Sarata, Chauhan, S., Bhattacharya, A., Chary, K., Govil, G., Kumar, Anil, Pellecchia, Maurizio, Zuiderweg, Erik, Kawano, Keiichi, Aizawa, Tomoyasu, Fujitani, Naoki, Hayakawa, Yoichi, Ohnishi, Atsushi, Ohkubo, Tadayasu, Kumaki, Yasuhiro, Hikichi, Kunio, Nitta, Katsutoshi, Rani Parvathy, V., Chary, K., Kini, R., Govil, G., Koshiba, Takumi, Kobashigawa, Yoshihiro, Yao, Min, Demura, Makoto, Nakagawa, Astushi, Tanaka, Isao, Kuwajima, Kunihiro, Nitta, Katsutoshi, Linge, Jens, Donoghue, Seán, Nilges, Michael, Chakshusmathi, G., Ratnaparkhi, Girish, Madhu, P., Varadarajan, R., Tetreau, C., Tourbez, M., Lavalette, D., Manno, M., Biagio, P., Martorana, V., Emanuele, A., Vaiana, S., Bulone, D., Palma-Vittorelli, M., Palma, M., Trivedi, V., Cheng, S., Chien, W., Yang, S., Francis, S., Chang, D., Batra, Renn, Geeves, Michael, Manstein, Dietmar, Trvlska, Joanna, Grochowski, Pawel, Geller, Maciej, Ginalski, K., Grochowski, P., Lesyng, B., Lavalette, P., Tetreau, C., Tourbez, M., Blouquit, Y., Roccatano, D., Amadei, A., Nola, A., Berendsen, H., Ho, Bosco, Curmi, P., Berry, H., Lairez, D., Pauthe, E., Pelta, J., Kothekar, V., Sahi, Shakti, Srinivasan, M., Singh, Anil, Madhusudnan, Kartha, Nandel, Fateh, Kaur, Harpreet, Nandel, Fateh, Singh, Balwinder, Jain, D., Feenstra, K., Berendsen, Herman, Tama, F., Sanejouand, Y., Go, N., Sharma, Deepak, Sharma, Sunita, Pasha, Santosh, Brahmachari, Samir, Viiavaraghavan, R., Makker, Jyoti, Dey, Sharmisllia, Kumar, S., Singh, T., Lakshmikanth, G., Krishnamoorthy, G., Mazhul, V., Zaitseva, E., Kierdaszuk, Borys, Widengren, J., Terry, B., Mets, Ü., Rigler, R., Swaminathan, R., Thamotharan, S., Yathindra, N., Shibata, Y., Chosrowjan, H., Mataga, N., Morisima, I., Chakraharty, Tania, Xiao, Ming, Cooke, Roger, Selvin, Paul, Branca, C., Faraone, A., Magazù, S., Maisano, G., Migliardo, P., Villari, V., Behere, Digambar, Deva, M., Brunori, M., Cutruzzolà, F., Gibson, Q., Savino, C., Travaglini-Allocatelli, C., Vallone, B., Prasad, Swati, Mazumdar, Shyamalava, Mitra, Samaresh, Soto, P., Fayad, R., Sukovataya, I., Tyulkova, N., Mamedov, Sh., Aktas, B., Canturk, M., Aksakal, B., Yilgin, R., Bogutska, K., Miroshnichenko, N., Chacko, S., DiSanto, M., Hypolite, J., Zheng, Y-M., Wein, A., Wojciechowski, M., Grycuk, T., Antosiewicz, J., Lesyng, B., Ceruso, Marc, Nola, Alfredo, Bandvopadhvay, Subhasis, Chatterjee, Bishnu, Choudhury, Devapriva, Thompson, Andrew, Stojanoff, Vivian, Pinkner, Jerome, Hultgren, Scott, Khight, Stefan, Flatters, Delphine, Goodfellow, Julia, Takazawatt, Fumi, Kanehisa, Minoru, Sasai, Masaki, Nakamura, Hironori, Sasai, Masaki, Han, Wang, Zheng, Yuan, Xin, Wang, Min, Pan, Bhakuni, Vlnod, Kulkarni, Sangeeta, Ahmad, Atta, Prakash, Koodathingal, Prajapati, Shashi, Surin, Alexey, Matsumoto, Tomoharu, Yang, Li, Nakagawa, Yuki, Kimura, Kazumoto, Amemiya, Yoshiyuki, Semisotnov, Gennady, Kihara, Hiroshi, Tayyab, Saad, Muzammil, Salman, Kumar, Yogesh, Kulkarni, Sangeeta, Prajapati, Shashi, Prakash, Koodathingal, Ahmad, Atta, Bhakuni, Vinod, Sundd, Monica, Kundu, Suman, Jagannadham, M., Kundu, Suman, Sundd, Monica, Jagannadham, Medicherla, Chandani, Bina, Dhar, Ruby, Sinha, Lalankumar, 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Ananthanarayanan, Vettai, Alirzayeva, E., Baba-Zade, S., Gromiha, M., Oobatake, M., Kono, H., An, J., Uedaira, H., Sarai, A., Takano, Kazufumi, Yamagata, Yuriko, Yutani, Katsuhide, Jas, Gouri, Muñoz, Victor, Hofrichter, James, Eaton, William, Penoyar, Jonathan, Srikrishnan, Thamarapu, Lo Verde, Philip, Kardos, J., Bódi, Á., Venekei, I., Závodszky, P., Gráf, L., Szilágyi, András, Závodszky, Péter, Allan, R., Walshaw, J., Woolfson, D., Funahashi, Jun, Takano, Kazufumi, Yamagata, Yuriko, Yutani, Katsuhide, Gupta, Savan, Mazumdar, Shyamalava, Di Nola, A., Mangoni, M., Roccatano, P., Ramachandraiah, Gosu, Chandra, Nagasuma, Kothekar, V., Srinivasan, M., Sahi, Shakti, Chakraborty, S., Bhattacharya, S., Bera, A., Ghosh, S., Pal, A., Haldar, U., Mukhopadhyay, B., Baneriee, Asok, Ciani, Barbara, Woolfson, Derek, Nair, Usha, Kaur, Kanwal, Salunke, Dinakar, Swaminathan, Chittoor, Surolia, Avadhesha, Rigler, R., Pramanik, A., Jonasson, P., Kratz, G., Jansson, O., Nygren, P., Ståhl, S., Ekberg, K., Johansson, B., Uhlén, S., Uhlén, M., Jörnvall, H., Wahren, J., Welfle, Karin, Misselwitz, Rolf, Höhne, Wolfgang, Welfle, Heinz, Mazhul, V., Zaitseva, E., Mitskevich, L., Fedurkina, N., Kurganov, B., Jarori, Gotam, Maity, Haripada, Guharay, J., Sengupta, B., Sengupta, P., Sridevi, K., Kasturi, S., Gupta, S., Agarwal, Gunjan, Kwong, Suzanne, Briehl, Robin, Ismailova, O., N, Tyulkova, Hariharan, C., Pines, D., Pines, E., Zamai, M., Cohen-Luria, R., Yayon, A., Parola, A., Padya, M., Spooner, G., Woolfeon, D., Bakshi, Panchan, Sharma, Deepak, Sharma, Sunita, Bharadwaj, D., Pasha, Santosh, Sharma, U., Srivastava, N., Barthwal, R., Jagannathan, N., Matsuda, Keiko, Nishioka, Takaaki, Go, Nobuhiro, Aita, T., Urata, S., Husimi, Y., Majumder, Mainak, Chatterjee, Bishnu, Abrescia, Nicola, Malinina, Lucy, Subirana, Juan, Aymami, Juan, Eritxa, Ramón, Coll, Miquel, Premraj, B., Yathindra, N., Thenmalarchelvi, R., Yathindra, N., Kumar, P., Gautham, N., Kan, Lou, Ming-Hou, Lin, Shwu-Bin, Sana, Tapas, Roy, Kanal, Bruant, N., Flatters, D., Lavery, R., Genest, D., Rons, Remo, Sklenar, Heinz, Lavery, Richard, Kundu, Sudip, Bhattacharyya, Dhananjay, Bandyopadhyay, Debashree, Thakur, Ashoke, Majumdar, Rabi, Barceló, F., Portugal, J., Ramanathan, Sunita, Chary, K., Rao, B., Gliosli, Mahua, Kumar, N., Varshney, Umesh, Chary, K., Pataskar, Shashank, Brahmachari, Samir, Sarojini, R., Selvasekarapandian, S., Kolandaivel, P., Sukumar, S., Selvasekarapandian, S., Sarojini, R., Kolmdaivel, P., Sukumar, S., Sarojini, R., Selvasekarapandian, S., Kolandaivel, P., Sukumar, S., Selvasekarapandian, S., Sarojini, R., Kolandaivel, P., Sukumar, S., Maiti, Motilal, Sen, Anjana, Das, Suman, Terra, Elisa, Suraci, Chiara, Diviacco, Silvia, Quadrifoglio, Franco, Xodo, Luigi, Bandyopadhyay, Debashree, Bhattacharyya, Dhananjay, Kundu, Sudip, Thakur, Ashoke, Das, Suman, Ray, Arghya, Maiti, Motilal, Karthikeyan, G., Chary, Kandala, Rao, Basuthkar, Mujeeb, Anwer, James, Thomas, Kasyanenko, N., Haya, E., Bogdanov, A., Zanina, A., Bugs, M., Cornélio, M., Srikrishnan, Thamarapu, Tolstorukov, M., Sanval, Nitish, Tiwari, S., Tiwari, S., Sanyal, Nitish, Choudhury, Mihir, Kumar, Devesh, Sanyal, Nitish, Patel, P., Bhavesh, Neel, Hosur, R., Gabrielian, Anna, Wennmalm, Stefan, Edman, Lars, Rigler, Rudolf, Constantinescu, B., Radu, L., Radulcscu, I., Gazdaru, D., Wärmländer, Sebastian, Leijon, Mikael, Aoki, Setsuyuki, Kondo, Takao, Ishiura, Masahiro, Pashinskaya, V., Kosevich, M., Shelkovsky, V., Blagoy, Yu., Wang, Ji-hua, Malathi, R., Chandrasekhar, K., Premraj, B., Patel, P., Kandimalla, E., Agrawal, S., Hosur, R., Yathindra, N., Rastogi, V., Palafox, M., Singh, Chatar, Beniaminov, A., Bondarenko, S., Zdobnov, E., Minyat, E., Ulyanov, N., Ivanov, V., Singh, J., Sonawane, Kailas, Grosjean, Henri, Tewari, Ravindra, Sonavane, Uddhavesh, Morin, Annie, Grosjean, Henri, Tewari, Ravindra, Doherty, Elizabeth, Doudna, Jennifer, Tochio, H., Sato, S., Matsuo, H., Shirakawa, M., Kyogoku, Y., Javaram, B., Dixit, 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Visser, A., Dyubko, T., Ogihara, Toshihiko, Mishima, Kiyoshi, Shvaleva, A., Radenović, N., Minić, P., Jeremić, M., Radenović, Č., Aripov, T., Tadjibaeva, E., Vagina, O., Zamaraeva, M., Salakhutdinov, B., Cole, A., Poppofl, M., Naylor, C., Titball, R., Basak, A., Eaton, J., Naylor, C., Justin, N., Moss, D., Titball, R., Basak, A., Nomura, F., Nagata, M., Ishjkawa, S., Takiguchi, K., Takahashi, S., Hotani, H., Obuchi, Kaoru, Staudegger, Erich, Kriechbaum, Manfred, Lehrer, Robert, Waring, Alan, Lohner, Karl, Gangl, Susanne, Mayer, Bernd, Köhler, Gottfried, Shobini, J., Mishra, A., Guttenberg, Z., Lortz, B., Hu, B., Sackmann, E., Kozlova, N., Lukyanenko, L., Antonovich, A., Slobozhanina, E., Chernitsky, E., Krylov, Andrey, Antonenko, Yuri, Kotova, Elena, Yaroslavov, Alexander, Ghosh, Subhendu, Bera, Amal, Das, Sudipto, Urbánková, Eva, Jelokhani-Niaraki, Masood, Freeman, Karl, Jezek, Petr, Usmanov, P., Ongarbaev, A., Tonkikh, A., Pohl, Peter, Saparov, Sapar, Harikumar, P., Reeves, J., Rao, 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F., Tahradník, Ivan, Pavelková, Jana, Zahradniková, Alexandra, Zhorov, Boris, Ananthanaravanan, Vettai, Michailov, M., Neu, E., Seidenbusch, W., Gornik, E., Martin, D., Welscher, U., Weiss, D., Pattnaik, B., Jellali, A., Forster, V., Hicks, D., Sahel, J., Dreyfus, H., Picaud, S., Wang, Hong-Wei, Sui, Sen-fang, Luther, Pradeep, Barry, John, Morris, Ed, Squire, John, Sundari, C., Balasubramanian, D., Veluraia, K., Christlet, T., Suresh, M., Berry, H., Pelta, J., Lairez, D., Laretta-Garde, V., Krilov, Dubravka, Stojanović, Nataša, Herak, Janko, Jasuja, Ravi, Ivanova, Maria, Mirchev, Rossen, Ferrone, Frank, Stopar, David, Spruijt, Ruud, Wolfs, Cor, Hemminga, Marcus, Arcovito, G., Spirito, M., Sui, Sen-fang, Wang, Hong-Wei, Agrawal, Rajendra, Heagle, Amy, Penczek, Pawel, Grassucci, Robert, Frank, Joachim, Sharma, Manjuli, Jeyakumar, Loice, Fleischer, Sidney, Wagenknecht, Terence, Knupp, Carlo, Munro, Peter, Luther, Pradeep, Ezra, Eric, Squire, John, Ichihara, Koji, Kitazawa, Hidefumi, Iguchi, Yusuke, Hotani, Hirokazu, Itoh, Tomohiko, Pifat, Greta, Kveder, Marina, Pečar, Slavko, Schara, Milan, Nair, Deepak, Singh, Kavita, Rao, Kanury, Salunke, Dinakar, Kaur, Kanwaljeet, Jain, Deepti, Sundaravadivel, B., Goel, Manisha, Salunke, D., Kovalenko, E., Semenkova, G., Cherenkevich, S., Lakshmanan, T., Sriram, D., Srinivasan, S., Loganathan, D., Ramalingam, T., Lebrón, J., Bjorkman, P., Singh, A., Gayatri, T., Jain, Deepti, Kaur, Kanwaljeet, Sundaravadivel, B., Salunke, Dinakar, Caffarena, Ernesto, Grigera, J., Bisch, Paulo, Kiessling, V., Fromherz, P., Rao, K., Gaikwad, S., Khan, M., Suresh, C., Kaliannan, P., Gromiha, M., Elanthiraiyan, M., Chadha, K., Payne, J., Ambrus, J., Nair, M., Nair, Madhavan, Mahajan, S., Chadha, K., Hewitt, R., Schwartz, S., Bourguignon, J., Faure, M., Cohen-Addad, C., Neuburger, M., Ober, R., Sieker, L., Macherel, D., Douce, R., Gurumurthy, D., Velmurugan, S., Lobo, Z., Srivastava, Sudha, Phadke, Ratna, Govil, Girjesh, Desai, Prashant, Coutinho, Evans, Guseinova, I., Suleimanov, S., Zulfugarov, I., Novruzova, S., Aliev, J., Ismayilov, M., Savchenko, T., Alieva, D., Ilík, Petr, Kouřil, Roman, Bartošková, Hana, Nauš, Jan, Gaikwad, Jvoti, Thomas, Sarah, Vidyasagar, P., Garab, G., Simidjiev, I., Rajagopal, S., Várkonyi, Zs., Stoylova, S., Cseh, Z., Papp, E., Mustárdy, L., Holzenburg, A., Bruder, R., Genick, U., Woo, T., Millar, D., Gerwert, K., Getzoff, E., Jávorfí, Tamás, Garab, Győző, Naqvi, K., Kalimullah, Md., Gaikwad, Jyoti, Thomas, Sarah, Semwal, Manoj, Vidyasagar, P., Kouril, Roman, Ilik, Petr, Naus, Man, Pomozi, István, Horváth, Gábor, Wehner, Rüdiger, Bernard, Gary, Damjanović, Ana, Ritz, Thorsten, Schulten, Klaus, Jushuo, Wang, Jixiu, Shan, Yandao, Gong, Tingyun, Kuang, Nanming, Zhao, Freiberg, Arvi, Timpmann, Kõu, Ruus, Rein, Woodbury, Neal, Nemtseva, E., Kudryasheva, N., Sizykh, A., Shikhov, V., Nesterenko, T., Tikhomirov, A., Forti, Giorgio, Finazzi, Giovanni, Furia, Alberto, Barbagallo, Romina, Forti, Giorgio, Iskenderova, S., Agalarov, R., Gasanov, R., Osamu, Miyashita, Nobuhiro, G., Soni, R., Ramrakhiani, M., Yagi, Hiromasa, Tozawa, Kacko, Sekino, Nobuaki, Iwabuchi, Tomoyuki, Yoshida, Masasuke, Akutsu, Hideo, Avetisyan, A., Kaulen, A., Skulachev, V., Feniouk, B., Breyton, Cécile, Kühlbrandt, Werner, Assarsson, Maria, Gräslund, Astrid, Zsiros, O., Horváth, G., Mustárdy, L., Libisch, B., Gombos, Z., Budagovskaya, N., Kudryasheva, N., Harada, Erisa, Fukuoka, Yuki, Ohmura, Tomoaki, Fukunishi, Arima, Kawai, Gota, Watanabe, Kimitsuna, Akutsu, Hideo, Derganc, Jure, Božič, Bojan, Svetina, Saša, Žekš, Boštjan, Hoh, J., Li, Z., Rossmanith, G., Beer, E., Treijtel, B., Frederix, P., Blangè, T., Hénon, S., Galtet, F., Laurent, V., Planus, E., Isabey, D., Rath, L., Dash, P., Raval, M., Ramakrishnan, C., Balaram, R., Randic, Milan, Basak, Subhash, Vracko, Marjan, Nandy, Ashesh, Amic, Dragan, Beslo, Drago, Nikolic, Sonja, Trinajstic, Nenad, Walahaw, J., Woolfson, D., Lensink, Marc, Berendsen, Herman, Reddy, Boojala, Shindylov, Ilya, Bourne, Philip, Donnamaria, M., Xammar Oro, J., Grigera, J., Neagu, Monica, Neagu, Adrian, Praprotnik, Matej, Janežič, Dušanka, Mark, Pekka, Nilsson, Lennart, Martorana, V., Bulone, D., Fata, L., Manno, M., Biagio, P., Dardenne, Laurent, Werneck, Araken, Neto, Marçal, Bisch, Paulo, Kannan, N., Vishveshwara, S., Christlet, T., Veluraja, K., Grunwald, Gregory, Balaban, Alexandra, Basak, Kanika, Gute, Brian, Mills, Denise, Opitz, David, Balasubramanian, Krishnan, Mihalas, G., Lungeanu, Diana, Macovievici, G., Gruia, Raluca, Neagu, Monica, Cortez-Maghelly, C., Dalcin, B., Passos, E., Blesic, S., Ljubisavljevic, M., Milosevic, S., Stratimirovic, D., Bachhawat, Nandita, Mande, Shekhar, Ghosh, S., Nandy, A., Saito, Ayumu, Nishigaki, Koichi, Nishigaki, Koichi, Naimuddin, Mohammed, Mitaku, Shigeki, Hirokawa, Takatsugu, Ono, Mitsuo, Takaesu, Hirotomo, El Gohary, M., Ahmed, Abdalla, Eissa, A., Nakashima, Hiroshi, Nishikawa, Ken, Neagu, Monica, Neagu, Adrian, Raghava, G., Kurgalvuk, N., Goryn, O., Gerstman, Bernard, Gritsenko, E., Remmel, N., Maznyak, O., Kratasyuk, V., Esimbekova, E., Kratasyuk, V., Tchitchkan, D., Koulchitsky, S., Tikhonov, A., German, A., Pesotskaya, Y., Pashkevich, S., Pletnev, S., Kulchitsky, V., Duvvuri, Umamaheswar, Charagundla, Sridhar, Rizi, Rahim, Leigh, John, Reddy, Ravinder, Kumar, Mahesh, Coshic, O., Julka, P., Rath, O., Jagannathan, NR., Iliescu, Karina, Sajin, Maria, Moisoi, Nicolcta, Petcu, Ileana, Kuzmenko, A., Morozova, R., Nikolenko, I., Donchenko, G., Rahman, M., Ahmed, M., Naimuddin, Mohammed, Watanabe, Takehiro, Nishigaki, Koichi, Rubin, Y., Gilboa, H., Sharony, R., Ammar, R., Uretzky, G., Khubchandani, M., Mallick, H., Kumar, V., Jagannathan, N., Borthakur, Arijitt, Shapiro, Erik, Begum, M., Degaonkar, Mahaveer, Govindasamy, S., Dimitrov, Ivan, Kumosani, T., Bild, W., Stefanescu, I., Titescu, G., Iliescu, R., Lupusoru, C., Nastasa, V., Haulica, I., Khetawat, Gopal, Faraday, N., Nealen, M., Noga, S., Bray, P., Ananieva, T., Lycholat, E., Pashinskaya, V., Kosevich, MV., Stepanyan, S., Lycholat, E., Ananieva, T., Antonyuk, S., Khachatryan, R., Arakelian, H., Kumar, A., Ayrapetyan, S., Mkheyan, V., Agadjanyan, S., Khachatryan, A., Rajan, S., Kabaleeswaran, V., Malathi, R., Gopalakrishnan, Geetha, Govindachari, T., Ramrakhiani, Meera, Lowe, Phillip, Badley, Andrew, Cullen, David, Hermel, H., Schmahl, W., Möhwald, H., Singh, Anil, Majumdar, Nirmalya, Das, Joydip, Madhusudnan, Kartha, Dér, András, Kelemen, Loránd, Oroszi, László, Hámori, András, Ramsden, Jeremy, Ormos, Pál, Savitri, D., Mitra, Chanchal, Yanagida, Toshio, Esaki, Seiji, Kimura, Yuji, Nishida, Tomoyuki, Sowa, Yosiyuki, Radu, M., Koltover, V., Estrin, Ya., Kasumova, L., Bubnov, V., Laukhina, E., Dotta, Rajiv, Degaonkar, M., Raghunathan, P., Jayasundar, Rama, Jagannathan, N., Novák, Pavel, Marko, Milan, Zahradník, Ivan, Hirata, Hiroaki, Miyata, Hidetake, Ohki, Kazuo, Balaji, J., Sengupta, P., Maiti, S., Gonsalves, M., Barker, A., Macpherson, J., O’Hare, D., Winlove, C., Unwin, P., Sengupta, P., Phillip, R., Banerjee, S., Kumar, G., Maiti, S., Nagayaka, K., Danev, R., Sugitani, S., Murata, K., Gősch, Michael, Blom, H., Thyberg, P., Földes-Papp, Z., Björk, G., Holm, J., Heino, T., Rigler, Rudolf, Yokochi, Masashi, Inagaki, Fuyuhiko, Kusunoki, Masami, Matthews, E., Pines, J., Chukova, Yu., Koltover, Vitaly, Bansal, Geetanjali, Singh, Uma, Bansal, M., Nakata, Kotoko, Nakano, Tastuya, Kaminuma, Tsuguchika, Kang, B., Singh, U., Kirn, Bonn, Potocnik, Neja, Stare, Vito, Shukla, Latal, Natarajan, V., Devasagayam, T., Sastry, M., Kesavan, P., Sayfutdinov, R., Adamovich, V., Rogozin, D., Degermendzhy, A., Khetrapal, C., Ramanathan, K., Gowda, G., Ghimire, Kedar, Masaru, Ishida, Fujita, H., Ishiwata, S., Kishimoto, Y., Kawahara, S., Suzuki, M., Mori, H., Mishina, M., Kirino, Y., Ohshima, H., Dukhin, A., Shilov, V., Goetz, P., Sengupta, B., Guharay, J., Sengupta, P., and Mishra, R.

Published
1999
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130. Probing the alpha 1 beta 2 interface of human hemoglobin by mutagenesis. Role of the FG-C contact regions.

Author

Vallone, B, Bellelli, A, Miele, A E, Brunori, M, and Fermi, G

Abstract

The allosteric transition of hemoglobin involves an extensive reorganization of the alpha 1 beta 2 interface, in which two contact regions have been identified. This paper concerns at the effect of two mutations located in the "switch" (alpha C3 Thr --> Trp) and the "flexible joint" (beta C3 Trp --> Thr). We have expressed and characterized one double and two single mutants: Hb alpha T38W/beta W37T, Hb beta W37T, and Hb alpha T38W, whose structure has been determined by crystallography. We present data on: (i) the interface structure in the contact regions, (ii) oxygen and CO binding kinetics and cooperativity, (iii) dissociation rates of deoxy tetramers and association rates of deoxy dimers, and (iv) the effect of NaI on deoxy tetramer dissociation rate constant. All the mutants are tetrameric and T-state in the deoxygenated derivative. Reassociation of deoxygenated dimers is not modified by interface mutations. DeoxyHb alpha T38W/beta W37T dissociate much faster. We propose a binding site for I- at the switch region. The single mutants binds O2 cooperatively; the double one is almost non-cooperative, a feature confirmed by CO binding. The functional data, analyzed with the two-state model, indicate that these mutations reduce the value of the allosteric constant LO.

Published
1996

131. Reconstitution of cytochrome c oxidase in phospholipid vesicles containing polyvinylic polymers

Author

Sarti, P, Antonini, G, Malatesta, F, Vallone, B, Villaschi, S, Brunori, M, Hider, R C, and Hamed, K

Abstract

Cytochrome c oxidase was reconstituted in phospholipid vesicles in the presence of highly hydrophobic poly(vinyl alkanoate) polymers. Electron-microscopy observations demonstrated that polymer interaction with the lipid phase induces vesicles to adopt smaller diameters than those typical of standard proteoliposomes. Functional characterization of these polymer-proteoliposome structures indicates that the reconstitution of the enzyme proceeds efficiently without causing either scrambling of the protein orientation in the membrane or loss of respiratory control. A clear dependence of respiratory control ratio on vesicle size was also demonstrated, which is in agreement with a previous model proposed for control of activity of cytochrome c oxidase vesicles [Brunori, Sarti, Colosimo, Antonini, Malatesta, Jones & Wilson (1985) EMBO J. 4, 2365-2368].

Published
1989
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132. ATP-induced spectral changes in cytochrome c oxidase. A kinetic investigation

Author

Antonini, G, Malatesta, F, Sarti, P, Vallone, B, and Brunori, M

Abstract

Mixing ATP with soluble oxidized cytochrome c oxidase induces a spectral perturbation in the Soret region of the enzyme. This spectral perturbation is observed at ATP concentrations similar to those found to modulate the catalytic activity of cytochrome c oxidase [Malatesta, Antonini, Sarti & Brunori (1987) Biochem. J. 248, 161-165]. The process is reversible and corresponds to a simple binding with Kd = 0.2 mM at 25 degrees C. The absorbance change follows a first-order time course, and analysis of the ATP-concentration-dependence indicates the presence of a rate-limiting monomolecular step that governs the process. From the temperature-dependence of this process, studied at saturating concentrations of ATP, an activation energy of 44 kJ/mol (10.6 kcal/mol) was measured. The spectral perturbation also occurs when cytochrome c oxidase is reconstituted into artificial phospholipid vesicles, with equilibria and kinetics similar to those observed with the soluble enzyme. Mixing ATP with soluble oxidized cyanide-bound cytochrome c oxidase induces a different spectral perturbation, and the apparent affinity of ATP for the enzyme is substantially increased. There is no absolute specificity for ATP, because EGTA, inositol hexakisphosphate, sulphate and phosphate are all able to induce an identical spectral perturbation with the same kinetics, although the value of the apparent Kd is different for the various anions. The presence of Mg2+ ions decreases, in a saturation-dependent fashion, the apparent affinity of cytochrome c oxidase for ATP. The absorbance change can be correlated to the displacement of the Ca2+ bound to cytochrome c oxidase.

Published
1988
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136. The Monod-Wyman-Changeux allosteric model accounts for the quaternary transition dynamics in wild type and a recombinant mutant human hemoglobin

Author

Maurizio Brunori, Alessandro Spilotros, Matteo Levantino, Marco Cammarata, Antonio Cupane, Beatrice Vallone, Giorgio Schirò, Chiara Ardiccioni, Levantino, M, Spilotros, A, Cammarata, M, Schirò, G, Ardiccioni, C, Vallone, B, Brunori, M, Cupane, A, Institut de Physique de Rennes (IPR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS), Italian MIUR Grant PRIN 2008 to A.C. (Prot. 2008ZWHZJT), FIRB Proteomica 2007 to M.B. (Prot. RBRN07BMCT), Université de Rennes 1 (UR1), and Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Protein Conformation, cooperativity, MESH: Catalytic Domain, Cooperativity, 01 natural sciences, MESH: Recombinant Proteins, Hemoglobins, Protein structure, MESH: Protein Conformation, Catalytic Domain, protein structural dynamics, MESH: Allosteric Site, 0303 health sciences, Multidisciplinary, allostery, biology, MESH: Kinetics, Chemistry, Biological Sciences, Recombinant Proteins, [SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biophysics, MESH: Hemoglobins, Allosteric Site, MESH: Models, Molecular, Adult, MESH: Mutation, Stereochemistry, Kinetics, Allosteric regulation, 010402 general chemistry, 03 medical and health sciences, protein conformational changes, flash photolysis, hemoglobin, time-resolved wide angle x ray scattering, time-resolved x-ray scattering, Humans, 030304 developmental biology, time-resolved X-ray scattering, MESH: Humans, Wild type, Active site, MESH: Adult, Settore FIS/07 - Fisica Applicata(Beni Culturali, Ambientali, Biol.e Medicin), 0104 chemical sciences, protein conformational change, Allosteric enzyme, Mutation, biology.protein, Hemoglobin
Abstract

International audience; The acknowledged success of the Monod-Wyman-Changeux (MWC) allosteric model stems from its efficacy in accounting for the functional behavior of many complex proteins starting with hemoglobin (the paradigmatic case) and extending to channels and receptors. The kinetic aspects of the allosteric model, however, have been often neglected, with the exception of hemoglobin and a few other proteins where conformational relaxations can be triggered by a short and intense laser pulse, and monitored by time-resolved optical spectroscopy. Only recently the application of time-resolved wide-angle X-ray scattering (TR-WAXS), a direct structurally sensitive technique, unveiled the time scale of hemoglobin quaternary structural transition. In order to test the generality of the MWC kinetic model, we carried out a TR-WAXS investigation in parallel on adult human hemoglobin and on a recombinant protein (HbYQ) carrying two mutations at the active site [Leu(B10)Tyr and His(E7)Gln]. HbYQ seemed an ideal test because, although exhibiting allosteric properties, its kinetic and structural properties are different from adult human hemoglobin. The structural dynamics of HbYQ unveiled by TR-WAXS can be quantitatively accounted for by the MWC kinetic model. Interestingly, the main structural change associated with the R-T allosteric transition (i.e., the relative rotation and translation of the dimers) is approximately 10-fold slower in HbYQ, and the drop in the allosteric transition rate with ligand saturation is steeper. Our results extend the general validity of the MWC kinetic model and reveal peculiar thermodynamic properties of HbYQ. A possible structural interpretation of the characteristic kinetic behavior of HbYQ is also discussed.

Published
2012

137. An X-ray diffraction and X-ray absorption spectroscopy joint study of neuroglobin

Author

Giordano Mancini, Maurizio Brunori, Paola D'Angelo, Alessandro Arcovito, Stefano Della Longa, Beatrice Vallone, Tommaso Moschetti, Arcovito, A, Moschetti, T, D'Angelo, P, Mancini, Giordano, Vallone, B, Brunori, M, and DELLA LONGA, S.

Subjects
Absorption spectroscopy, Iron, Biophysics, Nerve Tissue Proteins, Heme, Biochemistry, Ferrous, Mice, exafs, hemeproteins, neuroprotection, synchrotron radiation, xanes, X-Ray Diffraction, Oxidation state, Escherichia coli, medicine, Animals, Histidine, Cloning, Molecular, Settore BIO/10 - BIOCHIMICA, Molecular Biology, Carbon Monoxide, X-ray absorption spectroscopy, Extended X-ray absorption fine structure, Chemistry, Spectrum Analysis, X-Rays, Recombinant Proteins, XANES, Globins, neuroglobin, EXAFS, Crystallography, Neuroglobin, Ferric, Oxidation-Reduction, Protein Binding, medicine.drug
Abstract

Neuroglobin (Ngb) is a member of the globin family expressed in the vertebrate brain, whose function is still under debate. A combined approach of X-ray Diffraction (XRD) on single crystal, together with Extended X-ray Absorption Fine Structure (EXAFS) and X-ray Absorption Near Edge Structure (XANES) in solution, has been undertaken to unequivocally establish the oxidation state of the heme iron in the crystal state, and to determine the fine structural details of the active site both in the bis-histidine and the CO-bound (NgbCO) states. The crystal structure of dithionite reduced mouse Ngb (at T=100K) has been compared with that of the ferric derivative previously reported (Vallone et al. 2004); no significant changes between the two were detected. Since the Fe K-edge X-ray Absorption Spectroscopy (XAS) method is sensitive to the oxidation state of the heme iron, we collected spectra in solution at 15K; moreover we acquired XANES data on a ferric bis-imidazole model compound, for comparison. The XAS data demonstrate that under X-ray the heme iron is photoreduced fairly rapidly. We conclude that the previously reported X-ray structure, which was collected on a crystal of ferric Ngb, very likely refers to a photoreduced species indistinguishable from the dithionite reduced protein. Results from the XAS analysis of NgbCO in solution are in good agreement with XRD data on the crystal, providing detailed parameters for the Fe-CO ligand binding geometry and pointing toward an 0.1-0.2 A increase of the Fe-proximal histidine bond relative to the ferrous bis-histidine state of the protein. However prolonged exposure of NgbCO to the X-ray beam is associated to XANES changes indicating rupture of the Fe-CO bond, probably due to secondary absorption events induced by X-rays. This result paves the way to novel experiments aimed at the structural characterization of the pentacoordinate state of ferrous Ngb, which is the only species competent in binding external ligands such as O2, CO or NO. Reference: Vallone, B., Nienhaus, K., Brunori, M., and G. U. Nienhaus. 2004. The structure of murine neuroglobin: Novel pathways for ligand migration and binding. Proteins. 56:85-92.

Published
2008

138. Reconstitution of cytochrome c oxidase into phospholipid vesicles: Effect of detergents

Author

Francesco Malatesta, Beatrice Vallone, Emilio D'Itri, Paolo Sarti, Giovanni Antonini, Vallone, B, Ditri, E, Antonini, Giovanni, Malatesta, F, and Sarti, P.

Subjects
chemistry.chemical_classification, Phospholipid vesicles, biology, Vesicle, Biophysics, Enzyme, Biochemistry, chemistry, Irreversible loss, Electrochemistry, biology.protein, Cytochrome c oxidase, Respiratory control, Physical and Theoretical Chemistry, Incubation
Abstract

Cytochrome c oxidase vesicles prepared using enzyme preparations subjected to cycles of freezing and thawing (+20 to −20°C) before reconstitution, display a decrease in respiratory control ratio (RCR); if the protein is incubated with detergents before reconstitution, a higher RCR value is restored. This effect is attributed to a detergent-mediated optimization of the structural assembly of the proteo-membrane unit occurring at the early stages of reconstitution. The same type of experiment carried out at different temperatures showed that incubation at 35°C for 30 min leads to a severe, irreversible loss of RCR.

Published
1990

141. ATP-Induced Spectral Perturbation in Cytochrome Oxidase

Author

Francesco Malatesta, Giovanni Antonini, Maurizio Brunori, Beatrice Vallone, Paolo Sarti, Antonini, Giovanni, Malatesta, F, Sarti, P, Vallone, B, and Brunori, M.

Subjects
Phytic Acid, biology, Chemistry, General Neuroscience, Cytochrome c, Cytochrome P450 reductase, General Biochemistry, Genetics and Molecular Biology, Electron Transport Complex IV, Kinetics, Adenosine Triphosphate, History and Philosophy of Science, Cytochrome C1, Biochemistry, biology.protein, Cytochrome c oxidase, Calcium, Egtazic Acid, Oxidation-Reduction
Published
1988

142. Is the internal electron transfer the rate-limiting step in the catalytic cycle of cytochrome c oxidase?

Author

M. Brunori, Francesco Malatesta, Beatrice Vallone, Giovanni Antonini, Paolo Sarti, Sarti, P, Antonini, Giovanni, Malatesta, F, Vallone, B, and Brunori, M.

Subjects
biology, Chemistry, General Neuroscience, Hydrogen-Ion Concentration, Rate-determining step, Combinatorial chemistry, General Biochemistry, Genetics and Molecular Biology, Electron Transport, Electron Transport Complex IV, Electron transfer, Kinetics, History and Philosophy of Science, Catalytic cycle, Cytochrome C1, Spectrophotometry, biology.protein, Cytochrome c oxidase

143. ATP-induced spectral changes in cytochrome c oxidase. A kinetic investigation

Author

Giovanni Antonini, Paolo Sarti, Maurizio Brunori, Francesco Malatesta, Beatrice Vallone, Antonini, Giovanni, Malatesta, F, Sarti, P, Vallone, B, and Brunori, M.

Subjects
chemistry.chemical_classification, biology, Stereochemistry, Cytochrome c, Kinetics, Cell Biology, Phosphate, Biochemistry, Catalysis, Absorbance, Electron Transport Complex IV, chemistry.chemical_compound, EGTA, Enzyme, Adenosine Triphosphate, chemistry, Spectrophotometry, biology.protein, Cytochrome c oxidase, Magnesium, Molecular Biology, Research Article
Abstract

Mixing ATP with soluble oxidized cytochrome c oxidase induces a spectral perturbation in the Soret region of the enzyme. This spectral perturbation is observed at ATP concentrations similar to those found to modulate the catalytic activity of cytochrome c oxidase [Malatesta, Antonini, Sarti & Brunori (1987) Biochem. J. 248, 161-165]. The process is reversible and corresponds to a simple binding with Kd = 0.2 mM at 25 degrees C. The absorbance change follows a first-order time course, and analysis of the ATP-concentration-dependence indicates the presence of a rate-limiting monomolecular step that governs the process. From the temperature-dependence of this process, studied at saturating concentrations of ATP, an activation energy of 44 kJ/mol (10.6 kcal/mol) was measured. The spectral perturbation also occurs when cytochrome c oxidase is reconstituted into artificial phospholipid vesicles, with equilibria and kinetics similar to those observed with the soluble enzyme. Mixing ATP with soluble oxidized cyanide-bound cytochrome c oxidase induces a different spectral perturbation, and the apparent affinity of ATP for the enzyme is substantially increased. There is no absolute specificity for ATP, because EGTA, inositol hexakisphosphate, sulphate and phosphate are all able to induce an identical spectral perturbation with the same kinetics, although the value of the apparent Kd is different for the various anions. The presence of Mg2+ ions decreases, in a saturation-dependent fashion, the apparent affinity of cytochrome c oxidase for ATP. The absorbance change can be correlated to the displacement of the Ca2+ bound to cytochrome c oxidase.

144. Binding of steroid substrates reveals the key to the productive transition of the cytochrome P450 OleP.

Author

Costanzo A, Fata F, Freda I, De Sciscio ML, Gugole E, Bulfaro G, Di Renzo M, Barbizzi L, Exertier C, Parisi G, D'Abramo M, Vallone B, Savino C, and Montemiglio LC

Subjects
Crystallography, X-Ray, Substrate Specificity, Lithocholic Acid chemistry, Lithocholic Acid metabolism, Binding Sites, Hydroxylation, Cytochrome P-450 Enzyme System metabolism, Cytochrome P-450 Enzyme System chemistry, Molecular Dynamics Simulation, Protein Binding, Testosterone metabolism, Testosterone chemistry, Bacterial Proteins metabolism, Bacterial Proteins chemistry, Hydrogen Bonding
Abstract

OleP is a bacterial cytochrome P450 involved in oleandomycin biosynthesis as it catalyzes regioselective epoxidation on macrolide intermediates. OleP has recently been reported to convert lithocholic acid (LCA) into murideoxycholic acid through a highly regioselective reaction and to unspecifically hydroxylate testosterone (TES). Since LCA and TES mainly differ by the substituent group at the C17, here we used X-ray crystallography, equilibrium binding assays, and molecular dynamics simulations to investigate the molecular basis of the diverse reactivity observed with the two steroids. We found that the differences in the structure of TES and LCA affect the capability of these molecules to directly form hydrogen bonds with N-terminal residues of OleP internal helix I. The establishment of these contacts, by promoting the bending of helix I, fosters an efficient trigger of the open-to-closed structural transition that occurs upon substrate binding to OleP and contributes to the selectivity of the subsequent monooxygenation reaction., Competing Interests: Declaration of interests The authors declare no competing interests., (Copyright © 2024 The Author(s). Published by Elsevier Inc. All rights reserved.)

Published
2024
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145. Structural insights into the DNA recognition mechanism by the bacterial transcription factor PdxR.

Author

Freda I, Exertier C, Barile A, Chaves-Sanjuan A, Vega MV, Isupov MN, Harmer NJ, Gugole E, Swuec P, Bolognesi M, Scipioni A, Savino C, Di Salvo ML, Contestabile R, Vallone B, Tramonti A, and Montemiglio LC

Subjects
Bacteria genetics, DNA metabolism, Protein Binding, Pyridoxal Phosphate metabolism, Bacillus clausii genetics, Bacterial Proteins metabolism, Transcription Factors metabolism
Abstract

Specificity in protein-DNA recognition arises from the synergy of several factors that stem from the structural and chemical signatures encoded within the targeted DNA molecule. Here, we deciphered the nature of the interactions driving DNA recognition and binding by the bacterial transcription factor PdxR, a member of the MocR family responsible for the regulation of pyridoxal 5'-phosphate (PLP) biosynthesis. Single particle cryo-EM performed on the PLP-PdxR bound to its target DNA enabled the isolation of three conformers of the complex, which may be considered as snapshots of the binding process. Moreover, the resolution of an apo-PdxR crystallographic structure provided a detailed description of the transition of the effector domain to the holo-PdxR form triggered by the binding of the PLP effector molecule. Binding analyses of mutated DNA sequences using both wild type and PdxR variants revealed a central role of electrostatic interactions and of the intrinsic asymmetric bending of the DNA in allosterically guiding the holo-PdxR-DNA recognition process, from the first encounter through the fully bound state. Our results detail the structure and dynamics of the PdxR-DNA complex, clarifying the mechanism governing the DNA-binding mode of the holo-PdxR and the regulation features of the MocR family of transcription factors., (© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.)

Published
2023
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146. Effect of Salts on the Conformational Dynamics of the Cytochrome P450 OleP.

Author

De Sciscio ML, Nardi AN, Parisi G, Bulfaro G, Costanzo A, Gugole E, Exertier C, Freda I, Savino C, Vallone B, Montemiglio LC, and D'Abramo M

Subjects
Protein Conformation, Molecular Dynamics Simulation, Salts, Cytochrome P-450 Enzyme System metabolism
Abstract

Cytochrome P450 OleP catalytic activity is strongly influenced by its structural dynamic conformational behavior. Here, we combine equilibrium-binding experiments with all-atom molecular dynamics simulations to clarify how different environments affect OleP conformational equilibrium between the open and the closed-catalytic competent-forms. Our data clearly show that at high-ionic strength conditions, the closed form is favored, and, very interestingly, different mechanisms, depending on the chemistry of the cations, can be used to rationalize such an effect.

Published
2023
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147. Probing the Role of Murine Neuroglobin CDloop-D-Helix Unit in CO Ligand Binding and Structural Dynamics.

Author

Exertier C, Sebastiani F, Freda I, Gugole E, Cerutti G, Parisi G, Montemiglio LC, Becucci M, Viappiani C, Bruno S, Savino C, Zamparelli C, Anselmi M, Abbruzzetti S, Smulevich G, and Vallone B

Subjects
Animals, Heme chemistry, Ligands, Mice, Neuroglobin metabolism, Neuroglobin chemistry
Abstract

We produced a neuroglobin variant, namely, Ngb CDless, with the excised CDloop- and D-helix, directly joining the C- and E-helices. The CDless variant retained bis-His hexacoordination, and we investigated the role of the CDloop-D-helix unit in controlling the CO binding and structural dynamics by an integrative approach based on X-ray crystallography, rapid mixing, laser flash photolysis, resonance Raman spectroscopy, and molecular dynamics simulations. Rapid mixing and laser flash photolysis showed that ligand affinity was unchanged with respect to the wild-type protein, albeit with increased on and off constants for rate-limiting heme iron hexacoordination by the distal His64. Accordingly, resonance Raman spectroscopy highlighted a more open distal pocket in the CO complex that, in agreement with MD simulations, likely involves His64 swinging inward and outward of the distal heme pocket. Ngb CDless displays a more rigid overall structure with respect to the wild type, abolishing the structural dynamics of the CDloop-D-helix hypothesized to mediate its signaling role, and it retains ligand binding control by distal His64. In conclusion, this mutant may represent a tool to investigate the involvement of CDloop-D-helix in neuroprotective signaling in a cellular or animal model.

Published
2022
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148. Neuroglobin, clues to function and mechanism.

Author

Exertier C, Montemiglio LC, Freda I, Gugole E, Parisi G, Savino C, and Vallone B

Subjects
Animals, Brain metabolism, Humans, Neuroglobin metabolism, Neurons metabolism, Globins chemistry, Globins genetics, Nerve Tissue Proteins chemistry, Nerve Tissue Proteins genetics
Abstract

Neuroglobin is expressed in vertebrate brain and belongs to a branch of the globin family that diverged early in evolution. Sequence conservation and presence in nervous cells of several taxa suggests a relevant role in the nervous system, with tight structural restraints. Twenty years after its discovery, a rich scientific literature provides convincing evidence of the involvement of neuroglobin in sustaining neuron viability in physiological and pathological conditions however, a full and conclusive picture of its specific function, or set of functions is still lacking. The difficulty of unambiguously assigning a precise mechanism and biochemical role to neuroglobin might arise from the participation to one or more cell mechanism that redundantly guarantee the functioning of the highly specialized and metabolically demanding central nervous system of vertebrates. Here we collect findings and hypotheses arising from recent biochemical, biophysical, structural, in cell and in vivo experimental work on neuroglobin, aiming at providing an overview of the most recent literature. Proteins are said to have jobs and hobbies, it is possible that, in the case of neuroglobin, evolution has selected for it more than one job, and support to cover for its occasional failings. Disentangling the mechanisms and roles of neuroglobin is thus a challenging task that might be achieved by considering data from different disciplines and experimental approaches., (Copyright © 2021 Elsevier Ltd. All rights reserved.)

Published
2022
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149. ALS2-Related Motor Neuron Diseases: From Symptoms to Molecules.

Author

Miceli M, Exertier C, Cavaglià M, Gugole E, Boccardo M, Casaluci RR, Ceccarelli N, De Maio A, Vallone B, and Deriu MA

Abstract

Infantile-onset Ascending Hereditary Spastic Paralysis, Juvenile Primary Lateral Sclerosis and Juvenile Amyotrophic Lateral Sclerosis are all motor neuron diseases related to mutations on the ALS2 gene, encoding for a 1657 amino acids protein named Alsin. This ~185 kDa multi-domain protein is ubiquitously expressed in various human tissues, mostly in the brain and the spinal cord. Several investigations have indicated how mutations within Alsin's structured domains may be responsible for the alteration of Alsin's native oligomerization state or Alsin's propensity to interact with protein partners. In this review paper, we propose a description of differences and similarities characterizing the above-mentioned ALS2-related rare neurodegenerative disorders, pointing attention to the effects of ALS2 mutation from molecule to organ and at the system level. Known cases were collected through a literature review and rationalized to deeply elucidate the neurodegenerative clinical outcomes as consequences of ALS2 mutations.

Published
2022
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150. Point Mutations at a Key Site Alter the Cytochrome P450 OleP Structural Dynamics.

Author

Montemiglio LC, Gugole E, Freda I, Exertier C, D'Auria L, Chen CG, Nardi AN, Cerutti G, Parisi G, D'Abramo M, Savino C, and Vallone B

Subjects
Binding Sites, Catalytic Domain, Crystallography, X-Ray, Protein Structure, Secondary, Substrate Specificity, Cytochrome P-450 Enzyme System metabolism, Point Mutation
Abstract

Substrate binding to the cytochrome P450 OleP is coupled to a large open-to-closed transition that remodels the active site, minimizing its exposure to the external solvent. When the aglycone substrate binds, a small empty cavity is formed between the I and G helices, the BC loop, and the substrate itself, where solvent molecules accumulate mediating substrate-enzyme interactions. Herein, we analyzed the role of this cavity in substrate binding to OleP by producing three mutants (E89Y, G92W, and S240Y) to decrease its volume. The crystal structures of the OleP mutants in the closed state bound to the aglycone 6DEB showed that G92W and S240Y occupied the cavity, providing additional contact points with the substrate. Conversely, mutation E89Y induces a flipped-out conformation of this amino acid side chain, that points towards the bulk, increasing the empty volume. Equilibrium titrations and molecular dynamic simulations indicate that the presence of a bulky residue within the cavity impacts the binding properties of the enzyme, perturbing the conformational space explored by the complexes. Our data highlight the relevance of this region in OleP substrate binding and suggest that it represents a key substrate-protein contact site to consider in the perspective of redirecting its activity towards alternative compounds.

Published
2021
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