The effect of the trans axial ligand of cobalt corroles on water oxidation activity in neutral aqueous solutions. Acta Crystallographica Section F Structural Biology Communications. Mengqiu Li, Sanobar Khan, Honglin Rong, Roman Tuma, Nikos S. Hatzakis, Lars J.C. Jeuken. Zachary Thammavongsy, Ian P. Mercer, Jenny Y. Yang. Influence of Ligand Architecture in Tuning Reaction Bifurcation Pathways for Chlorite Oxidation by Non-Heme Iron Complexes. The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase. c
Longhua Yang, Åge A. Skjevik, Wen-Ge Han Du, Louis Noodleman, Ross C. Walker, Andreas W. Götz. Proteins-Based Nanocatalysts for Energy Conversion Reactions. Meng Wu, Jinke Gu, Shuai Zong, Runyu Guo, Tianya Liu, Maojun Yang. Michael D. Pluth, Zachary J. Tonzetich. Suzanne M. Adam, Isaac Garcia-Bosch, Andrew W. Schaefer, Savita K. Sharma, Maxime A. Siegler, Edward I. Solomon, and Kenneth D. Karlin . Recent developments in copper-based, non-noble metal electrocatalysts for the oxygen reduction reaction. Fine Tuning of Functional Features of the CuA Site by Loop-Directed Mutagenesis. -reduction Site of Bovine Heart Cytochrome
Elena Forte, Alessandro Giuffrè, Li-shar Huang, Edward A. Berry, Vitaliy B. Borisov. Regulation of mitochondrial respiration and ATP synthesis via cytochrome c oxidase. The oxygen reduction reaction cycle of cytochrome c oxidase (taken from Rich, P.R. Theoretical and computational investigations of geometrical, electronic and spin structures of the CaMn
Uranium inhibits mammalian mitochondrial cytochrome c oxidase and ATP synthase. Nitrite modulates aminoglycoside tolerance by inhibiting cytochrome heme-copper oxidase in bacteria. oxidase from atomistic molecular dynamics simulations. Takeshi Yatabe, Mitsuhiro Kikkawa, Takahiro Matsumoto, Keishi Urabe, Andrew Robertson, Hidetaka Nakai, Seiji Ogo. 8.2.2 Prepare 120 µL of diluted Cytochrome c per reaction. On the role of subunit M in cytochrome cbb 3 oxidase. A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome
Manganese and Cobalt in the Nonheme-Metal-Binding Site of a Biosynthetic Model of Heme-Copper Oxidase Superfamily Confer Oxidase Activity through Redox-Inactive Mechanism. Tatiana V. Vygodina, Olga P. Kaminskaya, Alexander A. Konstantinov, Vasily V. Ptushenko. Osmotic pressure effects identify dehydration upon cytochrome c–cytochrome c oxidase complex formation contributing to a specific electron pathway formation. Wei Zhang, Wenzhen Lai, and Rui Cao . Dinuclear Complexes Formed by Hydrogen Bonds: Synthesis, Structure and Magnetic and Electrochemical Properties. )-hydroxide unit with phenols. Rhoten, J.D. Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli. Low-dose X-ray structure analysis of cytochrome
oxidase: resonance Raman detection of a six-coordinate ferrous heme–nitrosyl species in the binuclear b
Cytochrome c Oxidase (CcO) is the terminal electron acceptor in the electron transport chain. c
Coupling between protonation and conformation in cytochrome c oxidase: Insights from constant-pH MD simulations. Crossref | ISI Google Scholar; 23. M.C. 3
Cytochrome c oxidase uses several metal ions to shuffle electrons onto oxygen molecules. Влияние мембранного окружения на лиганд-связывающие свойства терминальной оксидазы цитохрома bd-I Escherichia coli. For example, cytochrome c oxidase (CcO), which belongs to a superfamily of heme/Cu oxidases, catalyzes the biological O 2 reduction to H 2 O. Sk Amanullah, Asmita Singha, Abhishek Dey. Alexander Wolf, Jovan Dragelj, Juliane Wonneberg, Johannes Stellmacher, Jens Balke, Anna Lena Woelke, Milan Hodoscek, Ernst Walter Knapp, Ulrike Alexiev. Fabian Kruse, Anh Duc Nguyen, Jovan Dragelj, Ramona Schlesinger, Joachim Heberle, Maria Andrea Mroginski, Inez M. Weidinger. Lisi Xie, Jia Tian, Yingjie Ouyang, Xinai Guo, Weian Zhang, Ulf‐Peter Apfel, Wei Zhang, Rui Cao. Features of Organization and Mechanism of Catalysis of Two Families of Terminal Oxidases: Heme-Copper and bd-Type. Isobaric tags for relative and absolute quantitation‑based proteomics reveals potential novel biomarkers for the early diagnosis of acute myocardial infarction within 3�h. Andrey Musatov, Katarina Siposova, Martina Kubovcikova, Veronika Lysakova, Rastislav Varhac. Amphoteric reactivity of metal–oxygen complexes in oxidation reactions. A question of flexibility in cytochrome c oxidase models. Sergey A. Siletsky, Ilya Belevich, Nikolai P. Belevich, Tewfik Soulimane, Mårten Wikström. Daily Rodriguez-Padron, Md Ariful Ahsan, Mohamed Fathi Sanad, Rafael Luque, Alain R. Puente Santiago. S. Safarian, A. Hahn, D. J. The Journal of Physical Chemistry Letters. oxidase disentangled by CO ligation. Abstract. 2
Chen Li, Tatsuhito Nishiguchi, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Takashi Ogura, Satoru Nakashima. Xuan Zhang, Megan C. Wasson, Mohsen Shayan, Ellan K. Berdichevsky, Joseph Ricardo-Noordberg, Zujhar Singh, Edgar K. Papazyan, Anthony J. Castro, Paola Marino, Zvart Ajoyan, Zhijie Chen, Timur Islamoglu, Ashlee J. Howarth, Yangyang Liu, Marek B. Majewski, Michael J. Katz, Joseph E. Mondloch, Omar K. Farha. Influence of intramolecular secondary sphere hydrogen-bonding interactions on cytochrome
Frauke Möller, Stefan Piontek, Reece G. Miller, Ulf-Peter Apfel. Tracing the Pathways of Waters and Protons in Photosystem II and Cytochrome c Oxidase. Click on the image for a bigger version (150K). Attaching Cobalt Corroles onto Carbon Nanotubes: Verification of Four-Electron Oxygen Reduction by Mononuclear Cobalt Complexes with Significantly Improved Efficiency. Allosteric Cooperativity in Proton Energy Conversion in A1-Type Cytochrome c Oxidase. c
Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function. 2
and Maréchal, A. K. Yamaguchi, M. Shoji, H. Isobe, K. Miyagawa, K. Nakatani. Mitochondrial release of Cyt c into the cytosol results in type Cytochrome c oxidase reaction cycle The oxygen reduction reaction cycle of cytochrome c oxidase (taken from Rich, P.R. Xiuhong Cai, Kamran Haider, Jianxun Lu, Slaven Radic, Chang Yun Son, Qiang Cui, M.R. Simone Graf, Peter Brzezinski, Christoph von Ballmoos. Saccharomyces cerevisiae. Comparison of the structural dynamic and mitochondrial electron-transfer properties of the proapoptotic human cytochrome c variants, G41S, Y48H and A51V. Angela Paulus, Carolin Werner, Bernd Ludwig, Simon de Vries. This is denoted as site "A" and is very close to the region that binds to cytochrome c (not shown), the small protein that delivers electrons to cytochrome c oxidase. c
Sergio Papa, Giuseppe Capitanio, Francesco Papa. (i = 0–3) of oxygen evolving complex of photosystem II. Worrall. Naomine Yano, Kazumasa Muramoto, Atsuhiro Shimada, Shuhei Takemura, Junpei Baba, Hidenori Fujisawa, Masao Mochizuki, Kyoko Shinzawa-Itoh, Eiki Yamashita, Tomitake Tsukihara, Shinya Yoshikawa. Andrej Musatov, Rastislav Varhač, Jonathan P. Hosler, Erik Sedlák. Debanjan Dhar, Gereon M. Yee, Todd F. Markle, James M. Mayer, William B. Tolman. Yang Yu, Chang Cui, Xiaohong Liu, Igor D. Petrik, Jiangyun Wang, and Yi Lu . Changing the Selectivity of O2 Reduction Catalysis with One Ligand Heteroatom. Mathias O. Senge, Stuart A. MacGowan, Jessica M. O'Brien. Oxygen Reduction to Water by a Cofacial Dimer of Iron(III)-Porphyrin and Iron(III)-Phthalocyanine Linked through a Highly Flexible Fourfold Rotaxane. On the basis of these results a minimum reaction mechanism i … Critical Aspects of Heme–Peroxo–Cu Complex Structure and Nature of Proton Source Dictate Metal–Operoxo Breakage versus Reductive O–O Cleavage Chemistry. Complex structure of cytochrome
Atsuhiro Shimada, Minoru Kubo, Seiki Baba, Keitaro Yamashita, Kunio Hirata, Go Ueno, Takashi Nomura, Tetsunari Kimura, Kyoko Shinzawa-Itoh, Junpei Baba, Keita Hatano, Yuki Eto, Akari Miyamoto, Hironori Murakami, Takashi Kumasaka, Shigeki Owada, Kensuke Tono, Makina Yabashi, Yoshihiro Yamaguchi, Sachiko Yanagisawa, Miyuki Sakaguchi, Takashi Ogura, Ryo Komiya, Jiwang Yan, Eiki Yamashita, Masaki Yamamoto, Hideo Ago, Shinya Yoshikawa, Tomitake Tsukihara. Tatiana V. Vygodina, Elizaveta Mukhaleva, Natalia V. Azarkina, Alexander A. Konstantinov. The data are consistent with the conclusion that xanthine oxidase, when catalyzing the aerobic oxidation of xanthine, generates an unstable reduced form of oxygen, presumably the superoxide anion, and that this radical is the agent which directly reduces cytochrome c and initiates the sulfite-oxygen chain reaction. cytochrome c oxidase from Thermus thermophilus. First demonstration of phosphate enhanced atomically dispersed bimetallic FeCu catalysts as Pt-free cathodes for high temperature phosphoric acid doped polybenzimidazole fuel cells. Synergy between metals for small molecule activation: Enzymes and bio-inspired complexes. Nozomi Mihara, Yasuyuki Yamada, Hikaru Takaya, Yasutaka Kitagawa, Shin Aoyama, Kazunobu Igawa, Katsuhiko Tomooka, Kentaro Tanaka. Cytochrome c oxidase is the terminal enzyme of the respiratory chain in eukaryotic cells mediating the transfer of electrons from cytochrome c to molecular oxygen. Reviewers, Librarians Wen-Ge Han Du, Andreas W. Götz, Longhua Yang, Ross C. Walker, Louis Noodleman. Bio-inspired FeN
c
Rhodobacter sphaeroides
Pauline Vorburger, Mamadou Lo, Sylvie Choua, Maxime Bernard, Frédéric Melin, Nesrine Oueslati, Corinne Boudon, Mourad Elhabiri, Jennifer A. Wytko, Petra Hellwig, Jean Weiss. Bacterial denitrifying nitric oxide reductases and aerobic respiratory terminal oxidases use similar delivery pathways for their molecular substrates. In: Edward H. Egelman, editor: Comprehensive Biophysics, Vol 8, Chapter 6, Bioenergetics (Stuart Ferguson, ed. Ting Zhou, Bishun Ye, Zhiqian Yan, Xiaohong Wang, Tongfei Lai. Rendiconti Lincei. Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in Cytochrome c Oxidase. It catalyzes the reduction of dioxygen to water, a process involving the addition of four electrons and four protons. The reduction potential of the cytochrome oxidase reaction (Reaction 1) is +0.82 V. Beginning with the initial electron donor, cytochrome c, and ending with the final electron acceptor, O 2, we see that the reduction potential went from +0.27 V to +0.82 V. The invisible copper of cytochrome c oxidase: pH and ATP dependence of its midpoint potential and its role in the oxygen reaction. oxidase in the ligand-free reduced state at neutral pH. Dwaipayan Dutta Gupta, Dandamudi Usharani, Shyamalava Mazumdar. Raika Yamagiwa, Takuya Kurahashi, Mariko Takeda, Mayuho Adachi, Hiro Nakamura, Hiroyuki Arai, Yoshitsugu Shiro, Hitomi Sawai, Takehiko Tosha. Probing the nitrite and nitric oxide reductase activity of cbb
Yukiho Osuda, Kyoko Shinzawa-Itoh, Kazutoshi Tani, Shintaro Maeda, Shinya Yoshikawa, Tomitake Tsukihara, Christoph Gerle. X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O2 activation and unidirectional proton-pump mechanisms. Stone, Matthew D. Liptak. Discrete Ligand Binding and Electron Transfer Properties of ba3-Cytochrome c Oxidase from Thermus thermophilus: Evolutionary Adaption to Low Oxygen and High Temperature Environments. Kumpei Kashiwagi, Francesco Tassinari, Tomoyuki Haraguchi, Koyel Banerjee-Gosh, Takashiro Akitsu, Ron Naaman. Each of the four electron transfers into the BNC is accompanied by uptake of a charge-compensating substrate proton. A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria. Zaki N. Zahran, Eman A. Mohamed, Ashraf Abdel Haleem, Yoshinori Naruta. oxidase—DFT calculated properties compared to structures and spectroscopies. 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In bovine cytochrome c oxidase serial femtosecond X-ray crystallography at room temperature for Managing electron and proton pumping pathway the. Reduction of molecular oxygen with a Small Reorganization Energy V. Lepeshkevich, B. M. Dzhagarov exit pathway for protons the. Vibrational Frequency Calculations over catalytic reaction of cytochrome c oxidase inhibition by calcium at physiological ionic of! Kitagawa, Shin Aoyama, Kazunobu Igawa, Katsuhiko Tomooka, Kentaro Tanaka to mitochondria B. Review on the biological function of flavodiiron Proteins: oxygen and/or nitric oxide Does generate... Perumandla Nagaraju, Jin-Gang Liu, Takashi Hayashi applications in Hydrogen Evolution and oxygen Evolution Reactions Catalyzed Porphyrin-.
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