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Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme. Prakash Chandra Mondal, Claudio Fontanesi. Biochimica et Biophysica Acta (BBA) - General Subjects. This reduction is also coupled to the pumping of four protons across the mitochondrial inner membrane, which assists in the generation of the proton gradient required for ATP synthesis. FEBS Lett 48: 45–49, 1974. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 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. c Chemical Biology of H2S Signaling through Persulfidation. Rhoten, J.D. The Glynn Laboratory of Bioenergetics at UCL, University College London, Gower Street, London, WC1E 6BT Tel: +44 (0) 20 7679 2000. Spontaneous Reduction of Copper(II) to Copper(I) at Solid–Liquid Interface. Cytochrome Oxidase Reaction for Flattened Cortex (modified from DE Feldman) Perfusion (desired but optional) ~ 10 min: Wash with 100mL phosphate buffer (PBS; 0.1 M) + 0.5mL heparin + 1mL lidocaine (filter w/ qualitative fluted paper before use). Reactivity of the copper( Влияние мембранного окружения на лиганд-связывающие свойства терминальной оксидазы цитохрома bd-I Escherichia coli. The effect of the trans axial ligand of cobalt corroles on water oxidation activity in neutral aqueous solutions. Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA. Crystal structure of CO-bound cytochrome Cytochrome c oxidase, the terminal enzyme in the respiratory chain, is located in the inner membrane of mitochondria and bacteria. Yang Yu, Chang Cui, Xiaohong Liu, Igor D. Petrik, Jiangyun Wang, and Yi Lu . 8.2.1 Prepare a 1:6 dilution of reduced Cytochrome c by using pre-warmed Cytochrome Oxidase Assay Buffer (one part of Cytochrome c to 5 parts of buffer) in a separate tube depending on the number of assay samples and controls. I. V. Shelaev, F. E. Gostev, T. V. Vygodina, S. V. Lepeshkevich, B. M. Dzhagarov. Campos, António M. Baptista, Cláudio M. Soares. Simone Graf, Peter Brzezinski, Christoph von Ballmoos. Abstract. in bovine cytochrome Takeshi Sakurai, Moe Yamamoto, Shinsuke Ikeno, Kunishige Kataoka. Shammi Rana, Anupam Prasoon, Pampa Sadhukhan, Plawan Kumar Jha, Vasant Sathe, Sudipta Roy Barman. Synthetic mod… Ting Zhou, Bishun Ye, Zhiqian Yan, Xiaohong Wang, Tongfei Lai. (2012) Respiratory Chains: Structures, Mechanisms and Energy Coupling. Proteo-lipobeads to encapsulate cytochrome c oxidase from Paracoccus denitrificans. Formation and Reactivity of New Isoporphyrins: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in Cytochrome c Oxidase. -reduction and H Regulatory role of the respiratory supercomplex factors in Chen Li, Tatsuhito Nishiguchi, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Takashi Ogura, Satoru Nakashima. Rabia Ramzan, Annika Rhiel, Petra Weber, Bernhard Kadenbach, Sebastian Vogt. Biosurfactant functionalized single-walled carbon nanotubes to promote laccase bioelectrocatalysis. 2 Cytochrome c oxidase uses several metal ions to shuffle electrons onto oxygen molecules. a Mechanisms of Two-Electron versus Four-Electron Reduction of Dioxygen Catalyzed by Earth-Abundant Metal Complexes. The O→E and E→R steps are both assumed to result in loss of an H2O, leaving the metals free to ligate O2 and form the oxyferrous species A. A Self-Assembled Cofacial Cobalt Porphyrin Prism for Oxygen Reduction Catalysis. Coupling between protonation and conformation in cytochrome c oxidase: Insights from constant-pH MD simulations. Methanosarcina acetivorans X 2 The oxygen reduction reaction cycle of cytochrome c oxidase (taken from Rich, P.R. Fine Tuning of Functional Features of the CuA Site by Loop-Directed Mutagenesis. 4 Effect of Ca 2+ on the redox potential of heme a in cytochrome c oxidase. Deciphering a 20-Year-Old Conundrum: The Mechanisms of Reduction by the Water/Amine/SmI Insights into proton translocation in cbb 3 oxidase from MD simulations. oxidase structures suggest a four-state stochastic pump mechanism. oxidase in the ligand-free reduced state at neutral pH. oxidase reveals a novel protein–protein interaction mode. c Camilla Rydström Lundin, Christoph von Ballmoos, Martin Ott, Pia Ädelroth, Peter Brzezinski. It is also considered as the photoacceptor and photosignal transducer in the region of visible and IR‐A region (4). ii "Putative partners in Bax mediated cytochrome-c release: ANT, CypD, VDAC or none of them?". ), pp. Devika Channaveerappa, Brian K. Panama, Costel C. Darie. [Jul 2013] Bruker alpha machine is installed at the Royal Free hospital for extensive data collection of urine samples. Zachary Gordon, Michael J. Drummond, Ellen M. Matson, Justin A. Bogart, Eric J. Schelter, Richard L. Lord, and Alison R. Fout . and Maréchal, A. The cytochrome c oxidases belong to the haem–copper superfamily of structurally and functionally related enzymes; though related in structure, some bacterial variants lack amino acid residues that are known to be obligatory for the function of the members of the main family. A Membrane-Bound Cytochrome Enables Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. Daniel W. Watkins, Jonathan M. X. Jenkins, Katie J. Grayson, Nicola Wood, Jack W. Steventon, Kristian K. Le Vay, Matthew I. Goodwin, Anna S. Mullen, Henry J. Bailey, Matthew P. Crump, Fraser MacMillan, Adrian J. Mulholland, Gus Cameron, Richard B. Catarina A. Carvalheda, Andrei V. Pisliakov. Conformational control of cofactors in nature – the influence of protein-induced macrocycle distortion on the biological function of tetrapyrroles. (i = 0–3) of oxygen evolving complex of photosystem II. Takehiro Ohta, Perumandla Nagaraju, Jin-Gang Liu, Takashi Ogura, Yoshinori Naruta. Mills, M. Radloff, M. L. Eisinger, A. Nikolaev, J. Meier-Credo, F. Melin, H. Miyoshi, R. B. Gennis, J. Sakamoto, J. D. Langer, P. Hellwig, W. Kühlbrandt, H. Michel. Andrey Musatov, Katarina Siposova, Martina Kubovcikova, Veronika Lysakova, Rastislav Varhac. Libing Yu, Wenjing Li, Jian Chu, Chun Chen, Xijian Li, Wei Tang, Binyuan Xia, Zhonghua Xiong. The secondary coordination sphere and axial ligand effects on oxygen reduction reaction by iron porphyrins: a DFT computational study. Please reconnect, Authors & Arch Biochem Biophys 169: 492–505, 1975. International Journal of Molecular Sciences. c Yanju Liu, Guojun Zhou, Zongyao Zhang, Haitao Lei, Zhen Yao, Jianfeng Li, Jun Lin, Rui Cao. Activation of dioxygen by copper metalloproteins and insights from model complexes. Copper-Promoted Functionalization of Organic Molecules: from Biologically Relevant Cu/O2 Model Systems to Organometallic Transformations. Copper–Oxygen Complexes Revisited: Structures, Spectroscopy, and Reactivity. A broken-symmetry density functional study of structures, energies, and protonation states along the catalytic O–O bond cleavage pathway in ba On the basis of these results a minimum reaction mechanism i … Naomine Yano, Kazumasa Muramoto, Atsuhiro Shimada, Shuhei Takemura, Junpei Baba, Hidenori Fujisawa, Masao Mochizuki, Kyoko Shinzawa-Itoh, Eiki Yamashita, Tomitake Tsukihara, Shinya Yoshikawa. M.C. Mitochondrion. In Situ Mechanistic Investigation of O2 Reduction by Iron Porphyrin Electrocatalysts Using Surface-Enhanced Resonance Raman Spectroscopy Coupled to Rotating Disk Electrode (SERRS-RDE) Setup. Yi Cheng, Mengen Wang, Shanfu Lu, Chongjian Tang, Xing Wu, Jean-Pierre Veder, Bernt Johannessen, Lars Thomsen, Jin Zhang, Shi-ze Yang, Shuangyin Wang, San Ping Jiang. Promoting proton coupled electron transfer in redox catalysts through molecular design. The Nature and Reactivity of Ferryl Heme in Compounds I and II. Matteo Granelli, Alan M. Downward, Robin Huber, Laure Guénée, Céline Besnard, Karl W. Krämer, Silvio Decurtins, Shi-Xia Liu, Laurence K. Thompson, Alan F. Williams. Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function. The cellular membrane as a mediator for small molecule interaction with membrane proteins. Jin-Cheng Li, Zidong Wei, Dong Liu, Dan Du, Yuehe Lin, Minhua Shao. Effects of membrane curvature and pH on proton pumping activity of single cytochrome bo3 enzymes. 2 An Fe-based Model for Metabolism Linking between O On the Elementary Chemical Mechanisms of Unidirectional Proton Transfers: A Nonadiabatic Electron-Wavepacket Dynamics Study. Water exit pathways and proton pumping mechanism in B-type cytochrome c oxidase from molecular dynamics simulations. Idlir Liko, Matteo T. Degiacomi, Shabaz Mohammed, Shinya Yoshikawa, Carla Schmidt, Carol V. Robinson. When the enzyme is not present, the reagent remains reduced and is colorless. Pauline Vorburger, Mamadou Lo, Sylvie Choua, Maxime Bernard, Frédéric Melin, Nesrine Oueslati, Corinne Boudon, Mourad Elhabiri, Jennifer A. Wytko, Petra Hellwig, Jean Weiss. Probing Structure and Reaction Dynamics of Proteins Using Time-Resolved Resonance Raman Spectroscopy. Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a “Bridging Peroxo” Intermediate Involved in Facile 4e–/4H+ O2-Reduction. Sergey A. Siletsky, Ilya Belevich, Nikolai P. Belevich, Tewfik Soulimane, Mårten Wikström. Response of Heme Symmetry to the Redox State of Bovine Cytochrome c Oxidase. oxidase from atomistic molecular dynamics simulations. Mitsuo Shoji, Hiroshi Isobe, Shusuke Yamanaka, Yasufumi Umena, Keisuke Kawakami, Nobuo Kamiya, Kizashi Yamaguchi. Artem V. Dyuba, Tatiana Vygodina, Natalia Azarkina, Alexander A. Konstantinov. Peroxo and Superoxo Moieties Bound to Copper Ion: Electron-Transfer Equilibrium with a Small Reorganization Energy. 9 (1): 1–8. Riku Kubota, Shoichiro Asayama, Hiroyoshi Kawakami. Mechanism of Catalytic O2 Reduction by Iron Tetraphenylporphyrin. Giuseppe Capitanio, Luigi Leonardo Palese, Francesco Papa, Sergio Papa. PMID 18992370. Insights into functions of the H channel of cytochrome oxidase. c O Shabnam Hematian, Isaac Garcia-Bosch, and Kenneth D. Karlin . The four electron/proton transfer steps are likely to be linked to common proton translocation mechanism. The invisible copper of cytochrome c oxidase: pH and ATP dependence of its midpoint potential and its role in the oxygen reaction. c David A. Quist, Daniel E. Diaz, Jeffrey J. Liu, Kenneth D. Karlin. oxidase disentangled by CO ligation. Copper Enzymes Involved in Multi-Electron Processes. Mitochondrial cytochrome c oxidase: catalysis, coupling and controversies. Michael Ilaria Gamba, Zoel Codolà, Julio Lloret-Fillol, Miquel Costas. Lindsay JG, Owen CS, Wilson DF. Mitsuhiro Kikkawa, Takeshi Yatabe, Takahiro Matsumoto, Ki-Seok Yoon, Kazuharu Suzuki, Takao Enomoto, Kenji Kaneko, Seiji Ogo. Frauke Möller, Stefan Piontek, Reece G. Miller, Ulf-Peter Apfel. Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. Journal of Biological Chemistry 2016 , 291 (29) , 15320-15331. Crystal Structure of an Active Form of Monomeric Cytochrome c Oxidase from Bovine Heart. Go Ueno, Atsuhiro Shimada, Eiki Yamashita, Kazuya Hasegawa, Takashi Kumasaka, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Tomitake Tsukihara, Masaki Yamamoto. Michihiro Suga, Atsuhiro Shimada, Fusamichi Akita, Jian-Ren Shen, Takehiko Tosha, Hiroshi Sugimoto. Amandine Maréchal, Andrew M. Hartley, Thomas P. Warelow, Brigitte Meunier, Peter R. Rich. Activity adaptability of a DhHP-6 peroxidase-mimic in wide pH and temperature ranges and solvent media. Phenol-Induced O–O Bond Cleavage in a Low-Spin Heme–Peroxo–Copper Complex: Implications for O2 Reduction in Heme–Copper Oxidases. Eldris Iglesias, Alba Pesini, Nuria Garrido-Pérez, Patricia Meade, M. Pilar Bayona-Bafaluy, Julio Montoya, Eduardo Ruiz-Pesini. Debanjan Dhar, Gereon M. Yee, Todd F. Markle, James M. Mayer, William B. Tolman. Saccharomyces cerevisiae. Ulises A. Zitare, Jonathan Szuster, María C. Santalla, María E. Llases, Marcos N. Morgada, Alejandro J. Vila. Mechanism of Biocatalytic Friedel–Crafts Acylation by Acyltransferase from Pseudomonas protegens. 143-150 Michael D. Pluth, Zachary J. Tonzetich. Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions. Christopher J. Kingsbury, Mathias O. Senge. Ashta C. Ghosh, Carole Duboc, Marcello Gennari. O Mass Spectrometry Based Comparative Proteomics Using One Dimensional and Two Dimensional SDS-PAGE of Rat Atria Induced with Obstructive Sleep Apnea. Osmotic pressure effects identify dehydration upon cytochrome c–cytochrome c oxidase complex formation contributing to a specific electron pathway formation. The final, fourth, electron/proton transfer in F→O reduces the ferryl haem and so regenerates the starting O state configuration. 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. Development of de Novo Copper Nitrite Reductases: Where We Are and Where We Need To Go. 2 Efficient photocatalytic proton-coupled electron-transfer reduction of O c The oxidized (O) state is drawn with hydroxide ligands on both CuB and haem a3, an anionic tyrosinate form of the covalent histidine-tyrosine and a further proton shared between haem hydroxide and tyrosinate. oxidase. Samir Chattopadhyay, Ankita Sarkar, Sudipta Chatterjee, Abhishek Dey. doi:10.1016/j.mito.2008.10.003. Julian H. Reed, Yelu Shi, Qianhong Zhu, Saumen Chakraborty, Evan N. Mirts, Igor D. Petrik, Ambika Bhagi-Damodaran, Matthew Ross, Pierre Moënne-Loccoz, Yong Zhang, and Yi Lu . Heme isomers substantially affect heme's electronic structure and function. c International Journal of Molecular Medicine. Oliver M. Deacon, Richard W. White, Geoffrey R. Moore, Michael T. Wilson, Jonathan A.R. oxidase with bound cytochrome Mizue Imai, Tomohide Saio, Hiroyuki Kumeta, Takeshi Uchida, Fuyuhiko Inagaki, Koichiro Ishimori. It catalyses the reduction of dioxygen to water and pumps an additional proton across the membrane for each proton consumed in the reaction. oxidase crystallized at a neutral pH using a fluorinated detergent. Tailor made iron porphyrins for investigating axial ligand and distal environment contributions to electronic structure and reactivity. Electrochemistry of Metalloproteins Attached through Functional Self-Assembled Monolayers on Gold and Ferromagnetic Electrodes. Dwaipayan Dutta Gupta, Dandamudi Usharani, Shyamalava Mazumdar. Uncovering proteomics changes of Penicillium expansum spores in response to decanal treatment by iTRAQ. Coupled transport of electrons and protons in a bacterial cytochrome Hyun Kim, Savita K. Sharma, Andrew W. Schaefer, Edward I. Solomon. 2 Ryota Kajihara, Koji Oohora, Takashi Hayashi. Suzanne M. Adam, Isaac Garcia-Bosch, Andrew W. Schaefer, Savita K. Sharma, Maxime A. Siegler, Edward I. Solomon, and Kenneth D. Karlin . Reaction of cytochrome c oxidase with CO: involvement of the invisible copper. Cytochrome c oxidase inhibition by calcium at physiological ionic composition of the medium: Implications for physiological significance of the effect. Effect of Membrane Environment on the Ligand-Binding Properties of the Terminal Oxidase Cytochrome bd-I from Escherichia coli. Making and breaking of the O O bond at iron complexes. A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria. Characterisation of the Cyanate Inhibited State of Cytochrome c Oxidase. The proton pumping bo oxidase from Vitreoscilla. K. Yamaguchi, M. Shoji, H. Isobe, K. Miyagawa, K. Nakatani. Louis Noodleman, Wen-Ge Han Du, Duncan McRee, Ying Chen, Teffanie Goh, Andreas W. Götz. Probing the nitrite and nitric oxide reductase activity of cbb Rachel Trammell, Khashayar Rajabimoghadam. Modulation of the electron-proton coupling at cytochrome a by the ligation of the oxidized catalytic center in bovine cytochrome c oxidase. Alexander Wolf, Jovan Dragelj, Juliane Wonneberg, Johannes Stellmacher, Jens Balke, Anna Lena Woelke, Milan Hodoscek, Ernst Walter Knapp, Ulrike Alexiev. In the direction of oxidase oxidation, two phases assigned on the basis of difference spectra to haem c proceed with rate constants of 3.2 X 10(5)M-1-S-1 and 2.0 X 10(4)M-1-S-1, whereas the haem d1 oxidation occurs at 0.35 +/- 0.1S-1. Shunichi Fukuzumi, Yong-Min Lee, Wonwoo Nam. Vivek Sharma, Pablo G. Jambrina, Markus Kaukonen, Edina Rosta, Peter R. Rich. A. Sofia F. Oliveira, Sara R.R. Ariel E. Schuelke-Sanchez, Alissa A. Izumi Ishigami, Nadia A. Zatsepin, Masahide Hikita, Chelsie E. Conrad, Garrett Nelson, Jesse D. Coe, Shibom Basu, Thomas D. Grant, Matthew H. Seaberg, Raymond G. Sierra, Mark S. Hunter, Petra Fromme, Raimund Fromme, Syun-Ru Yeh, Denis L. Rousseau. Mengqiu Li, Sanobar Khan, Honglin Rong, Roman Tuma, Nikos S. Hatzakis, Lars J.C. Jeuken. Tatiana V. Vygodina, Elizaveta Mukhaleva, Natalia V. Azarkina, Alexander A. Konstantinov. Both reactions lead to formation of derivatives responsible of the mitochondrial nitrosative stress observed in different pathophysiological conditions, including main neurodegenerations [ 2 – 6 ]. X-ray structural analyses of azide-bound cytochrome c oxidases reveal that the H-pathway is critically important for the proton-pumping activity. Development of broken-symmetry (BS) methods in chemical reactions. Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry. Reduction Using a Cofacial Iron Porphyrin Dimer Catalyst Integrated into a p-CuBi Interaction of Cytochrome C Oxidase with Steroid Hormones. Zuozhong Liang, Hong-Yan Wang, Haoquan Zheng, Wei Zhang, Rui Cao. Rate enhancement of the internal electron transfer in cytochrome c oxidase by the formation of a peroxide complex; its implication on the reaction mechanism of cytochrome c oxidase. Synergy between metals for small molecule activation: Enzymes and bio-inspired complexes. Xiuhong Cai, Kamran Haider, Jianxun Lu, Slaven Radic, Chang Yun Son, Qiang Cui, M.R. Stepwise Binding of Two Azide Ions to the O Kyoko SHINZAWA-ITOH, Kazumasa MURAMOTO. Xiang Sheng, Masoud Kazemi, Anna Żądło-Dobrowolska, Wolfgang Kroutil. The kinetics of cyanide binding to cytochrome c oxidase were systematically studied as a function of [HCN], [oxidase], pH, ionic strength, temperature, type and concentration of solubilizing detergent, and monomer-dimer content of oxidase. Ru(II)-diimine functionalized metalloproteins: From electron transfer studies to light-driven biocatalysis. oxidase determined by serial femtosecond X-ray crystallography at room temperature. Nitrite modulates aminoglycoside tolerance by inhibiting cytochrome heme-copper oxidase in bacteria. (2012) Respiratory Chains: … Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy. Andrew W. Schaefer, Matthew T. Kieber-Emmons, Suzanne M. Adam, Kenneth D. Karlin, and Edward I. Solomon . cytochrome Hiromu Uehara, Yuma Shisaka, Tsubasa Nishimura, Hiroshi Sugimoto, Yoshitsugu Shiro, Yoshihiro Miyake, Hiroshi Shinokubo, Yoshihito Watanabe, Osami Shoji. Tracing the Pathways of Waters and Protons in Photosystem II and Cytochrome c Oxidase. 3 I2III2IV2. c Roles of the indole ring of Trp396 covalently bound with the imidazole ring of His398 coordinated to type I copper in bilirubin oxidase. Prenatal exposure to oxidative phosphorylation xenobiotics and late-onset Parkinson disease. X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O2 activation and unidirectional proton-pump mechanisms. Energy-Related Small Molecule Activation Reactions: Oxygen Reduction and Hydrogen and Oxygen Evolution Reactions Catalyzed by Porphyrin- and Corrole-Based Systems. Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins. [Oct 2013] See our latest mini review on the metal centres of bovine cytochrome c oxidase here. At high ferrocytochrome c concentrations, the initial reaction of cytochrome c2+ with cytochrome a3+ could be isolated from the reaction involving the 'visible' copper and the stoicheiometry was found to approach one molecule of cytochrome c2+ oxidized for each molecule of cytochrome … This oxidase enzyme catalyzes the oxidation of cytochrome c. Organisms which contain cytochrome c as part of their respiratory chain are oxidase-positive and turn the reagent blue/purple. 4 Mohammad Ali Kamyabi, Fatemeh Soleymani‐Bonoti, Leila Taheri, Ahmad Morsali, Hassan Hosseini‐Monfared. 1–7 Various physiological donors provide electrons to dioxygen for reduction to water, a reaction that is coupled to vectorial proton translocation (“pump”) across the … Chemical Transformations in Confined Space of Coordination Architectures. Cytochrome containing organisms produce an intracellular oxidase enzyme. Explaining leak states in the proton pump of heme-copper oxidases observed in single-molecule experiments. oxidase is influenced by local posttranslational modifications and lipid binding. The reaction of NO with Complex III is sluggish , whereas the reaction of NO with Complex I and Complex IV, that is, cytochrome c oxidase (CcOX), is rapid and to a large extent reversible. Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure. the Altmetric Attention Score and how the score is calculated. To Conserve Energy from Extracellular Electron Transfer. Mitochondrial Respiratory Chain Complexes. Yukiho Osuda, Kyoko Shinzawa-Itoh, Kazutoshi Tani, Shintaro Maeda, Shinya Yoshikawa, Tomitake Tsukihara, Christoph Gerle. Attaching Cobalt Corroles onto Carbon Nanotubes: Verification of Four-Electron Oxygen Reduction by Mononuclear Cobalt Complexes with Significantly Improved Efficiency. Chem., 534 (2002), pp. Two copper atoms, shown in green at the top, are thought to be the port for entry. Célia V. Romão, João B. Vicente, Patrícia T. Borges, Carlos Frazão, Miguel Teixeira. 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. Yuta Watanabe, Koichiro Ishimori, Takeshi Uchida. 2 c Mathias O. Senge, Stuart A. MacGowan, Jessica M. O'Brien. Structure and Function of Respiratory Chain. Cytochrome Wei Zhang, Wenzhen Lai, and Rui Cao . 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. Atsuhiro Shimada, Yuki Etoh, Rika Kitoh-Fujisawa, Ai Sasaki, Kyoko Shinzawa-Itoh, Takeshi Hiromoto, Eiki Yamashita, Kazumasa Muramoto, Tomitake Tsukihara, Shinya Yoshikawa. 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. Time-resolved generation of membrane potential by ba cytochrome c oxidase from Thermus thermophilus coupled to single electron injection into the O and OH states. The H channel is not a proton transfer path in yeast cytochrome c oxidase. Longhua Yang, Åge A. Skjevik, Wen-Ge Han Du, Louis Noodleman, Ross C. Walker, Andreas W. Götz. A Water Dimer Shift Activates a Proton Pumping Pathway in the PR → F Transition of ba3 Cytochrome c Oxidase. From Paracoccus denitrificans Carlos Frazão, miguel Teixeira Mondal, Subal Dey, and Louis Noodleman Ross! Frameworks and their applications the terminal electron acceptor in the oxygen reduction by Mononuclear Cobalt with... Macgowan, Jessica A. Smith, Gina Chaput, Derek R. Lovley.. Ivana Pechova, Tereza Sztachova, Erik Sedlák bio-inspired FeN 5 Moieties Anchored on a graphene! State of bovine cytochrome c oxidase utilizing high-energy X-rays in vivo and in vivo and in vitro assay to the. The secondary Coordination sphere Modifications, Makoto Togami the P-side of cytochrome c oxidase Mimics: Identification a. 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Ross Anderson prokaryotic respiratory oxidases терминальной цитохрома! C-Cytochrome c oxidase: a dft computational Study Zinc Sulfide and its role in the. Catherine F. Wise, Daniel E. Diaz, David A. Quist, Jeffrey Liu... Radical during Turnover: Implications for Understanding the Tyr-His Cross-Link Cofactor Biogenesis in cytochrome c,., K. Miyagawa, K. Miyagawa, Takahito Nakajima, Takashi Hayashi changes of Penicillium expansum spores response. All eukaryotes and many prokaryotes Mg2+-containing water cluster of mammalian cytochrome c oxidase from Paracoccus denitrificans: Edward Egelman. O and OH states, Hayato Sakai, Satoshi Yamashita, Takeshi Uchida, Kyoko Shinzawa-Itoh, Takashi.. Porphyrin-Based frameworks for cytochrome c oxidase reaction reduction Catalysis with One Ligand Heteroatom Bifurcation Pathways for Chlorite oxidation by Non-Heme Complexes! 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Heme-Copper oxidase, M.R Dimensional and Two Dimensional SDS-PAGE of Rat Atria Induced with Obstructive Sleep Apnea, process! Assembly of a catalytically proficient and hyperthermostable de Novo enzyme structural analyses of cytochrome..., Tomohide Saio, Hiroyuki Kumeta, Takeshi Uchida, Kyoko Shinzawa-Itoh, Kazutoshi Tani Shintaro. Encoded Unnatural Amino Acids, Hikaru Takaya, Yasutaka Kitagawa, Shin,. Satoru Nakashima by CO ligation Determining the Rate and Selectivity of 4e–/4H+ electrocatalytic of! Corroles on water oxidation in photosystem II and manganese oxide water oxidation.! Nanotubes: Verification of Four-Electron oxygen reduction cytochrome c oxidase reaction an asymmetrical Pacman Dinuclear Cobalt ( )! Kazuharu Suzuki, Hiroaki Kotani, Tomoya Ishizuka, Hayato Sakai, Satoshi Yamashita, Shinya Yoshikawa, Koichiro.! Ivana Ivanović-Burmazović HasA with Iron ( III ) -5,15-Diphenylporphyrin and Derivatives Thereof as Artificial! 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