cytochrome c oxidase reaction

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Riku Kubota, Shoichiro Asayama, Hiroyoshi Kawakami. and Maréchal, A. Xiang Sheng, Masoud Kazemi, Anna Żądło-Dobrowolska, Wolfgang Kroutil. Melanie A. Ehudin, Andrew W. Schaefer, Suzanne M. Adam, David A. Quist, Daniel E. Diaz, Joel A. Tang, Edward I. Solomon, Kenneth D. Karlin. Vivek Sharma, Pablo G. Jambrina, Markus Kaukonen, Edina Rosta, Peter R. Rich. Alexander Wolf, Jovan Dragelj, Juliane Wonneberg, Johannes Stellmacher, Jens Balke, Anna Lena Woelke, Milan Hodoscek, Ernst Walter Knapp, Ulrike Alexiev. Wataru Sato, Seiji Hitaoka, Takeshi Uchida, Kyoko Shinzawa-Itoh, Kazunari Yoshizawa, Shinya Yoshikawa, Koichiro Ishimori. Shina Hussain, Diann Andrews, and Bruce C. Hill . Uncovering proteomics changes of Penicillium expansum spores in response to decanal treatment by iTRAQ. Rabia Ramzan, Annika Rhiel, Petra Weber, Bernhard Kadenbach, Sebastian Vogt. oxidase from atomistic molecular dynamics simulations. Water exit pathways and proton pumping mechanism in B-type cytochrome c oxidase from molecular dynamics simulations. Michihiro Suga, Atsuhiro Shimada, Fusamichi Akita, Jian-Ren Shen, Takehiko Tosha, Hiroshi Sugimoto. Cytochrome c oxidase uses several metal ions to shuffle electrons onto oxygen molecules. oxidase. Mechanistic dichotomies in redox reactions of mononuclear metal–oxygen intermediates. The four electron/proton transfer steps are likely to be linked to common proton translocation mechanism. Tracing the Pathways of Waters and Protons in Photosystem II and Cytochrome c Oxidase. 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. Your Mendeley pairing has expired. 3 Coupling between protonation and conformation in cytochrome c oxidase: Insights from constant-pH MD simulations. Влияние мембранного окружения на лиганд-связывающие свойства терминальной оксидазы цитохрома bd-I Escherichia coli. Amanda N. Oldacre, Alan E. Friedman, and Timothy R. Cook . The mechanism of coupling between oxido-reduction and proton translocation in respiratory chain enzymes. 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. Hammett Relationship in Oxidase‐Mimicking Metal–Organic Frameworks Revealed through a Protein‐Engineering‐Inspired Strategy. Dispersive Single-Atom Metals Anchored on Functionalized Nanocarbons for Electrochemical Reactions. First demonstration of phosphate enhanced atomically dispersed bimetallic FeCu catalysts as Pt-free cathodes for high temperature phosphoric acid doped polybenzimidazole fuel cells. Debanjan Dhar, Gereon M. Yee, Todd F. Markle, James M. Mayer, William B. Tolman. Mechanisms of Two-Electron versus Four-Electron Reduction of Dioxygen Catalyzed by Earth-Abundant Metal Complexes. Amandine Maréchal, Jing-Yang Xu, Naho Genko, Andrew M. Hartley, Francis Haraux, Brigitte Meunier, Peter R. Rich. Mechanism of Catalytic O2 Reduction by Iron Tetraphenylporphyrin. Reversible dimerization of cytochrome c oxidase regulates mitochondrial respiration. a oxidase determined by serial femtosecond X-ray crystallography at room temperature. Click on the image for a bigger version (150K). The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase. 8.2.2 Prepare 120 µL of diluted Cytochrome c per reaction. A water-soluble supramolecular complex that mimics the heme/copper hetero-binuclear site of cytochrome Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure. 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. 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. Crossref | ISI Google Scholar; 23. c the Altmetric Attention Score and how the score is calculated. Development of de Novo Copper Nitrite Reductases: Where We Are and Where We Need To Go. A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase. c c Sudipta Chatterjee, Kushal Sengupta, Biswajit Mondal, Subal Dey, and Abhishek Dey . c Wataru Sato, Seiji Hitaoka, Kaoru Inoue, Mizue Imai, Tomohide Saio, Takeshi Uchida, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Kazunari Yoshizawa, Koichiro Ishimori. Amino acids located in the outer-sphere of the trinuclear copper center in a multicopper oxidase, CueO as the putative electron donor in the four-electron reduction of dioxygen. Cytochrome c oxidases (CcOs) are important members of the superfamily of heme/copper-containing terminal oxidases, which play a central role in the respiratory metabolism of both eukaryotic organisms as well as some aerobic bacteria. Aapo Malkamäki, Brigitte Meunier, Marco Reidelbach, Peter R. Rich, Vivek Sharma. Theoretical and computational investigations of geometrical, electronic and spin structures of the CaMn Functional and structural evaluation of bovine heart cytochrome c oxidase incorporated into bicelles. Activity adaptability of a DhHP-6 peroxidase-mimic in wide pH and temperature ranges and solvent media. c Zachary Thammavongsy, Ian P. Mercer, Jenny Y. Yang. Hiromu Uehara, Yuma Shisaka, Tsubasa Nishimura, Hiroshi Sugimoto, Yoshitsugu Shiro, Yoshihiro Miyake, Hiroshi Shinokubo, Yoshihito Watanabe, Osami Shoji. Ilaria Gamba, Zoel Codolà, Julio Lloret-Fillol, Miquel Costas. Ting Zhou, Bishun Ye, Zhiqian Yan, Xiaohong Wang, Tongfei Lai. It is also considered as the photoacceptor and photosignal transducer in the region of visible and IR‐A region (4). Active site rearrangement and structural divergence in prokaryotic respiratory oxidases. Rhodobacter sphaeroides https://doi.org/10.1021/acs.inorgchem.0c02400, https://doi.org/10.1021/acs.inorgchem.0c02408, https://doi.org/10.1021/acs.inorgchem.0c01379, https://doi.org/10.1021/acs.inorgchem.0c00724, https://doi.org/10.1021/acs.jmedchem.9b01069, https://doi.org/10.1021/acs.chemrev.9b00429, https://doi.org/10.1021/acs.inorgchem.9b02521, https://doi.org/10.1021/acs.inorgchem.9b01840, https://doi.org/10.1021/acs.accounts.9b00052, https://doi.org/10.1021/acs.chemrev.8b00368, https://doi.org/10.1021/acs.inorgchem.8b03244, https://doi.org/10.1021/acs.chemrev.8b00074, https://doi.org/10.1021/acs.jpclett.8b02844, https://doi.org/10.1021/acs.biochem.8b00459, https://doi.org/10.1021/acs.inorgchem.7b03067, https://doi.org/10.1021/acs.biochem.7b01194, https://doi.org/10.1021/acs.chemrev.7b00220, https://doi.org/10.1021/acs.chemrev.7b00373, https://doi.org/10.1021/acs.chemrev.7b00542, https://doi.org/10.1021/acs.chemrev.7b00664, https://doi.org/10.1021/acs.accounts.7b00463, https://doi.org/10.1021/acs.chemrev.7b00205, https://doi.org/10.1021/acs.inorgchem.7b02461, https://doi.org/10.1021/acs.biochem.7b00833, https://doi.org/10.1021/acs.chemrev.7b00257, https://doi.org/10.1021/acs.accounts.7b00192, https://doi.org/10.1021/acs.inorgchem.6b03071, https://doi.org/10.1021/acs.orglett.7b00531, https://doi.org/10.1021/acs.chemrev.6b00299, https://doi.org/10.1021/acs.chemrev.6b00636, https://doi.org/10.1021/acs.inorgchem.6b01384, https://doi.org/10.1021/acs.accounts.5b00265, https://doi.org/10.1016/j.apcatb.2020.119717, https://doi.org/10.1016/j.nanoen.2021.105798, https://doi.org/10.1016/j.ccr.2020.213760, https://doi.org/10.1016/j.ccr.2020.213606, https://doi.org/10.1016/j.envpol.2020.116377, https://doi.org/10.1016/j.ccr.2020.213615, https://doi.org/10.1038/s41598-020-60801-0, https://doi.org/10.1038/s42003-020-0991-4, https://doi.org/10.31857/S032097252012012X, https://doi.org/10.1134/S0006297920120123, https://doi.org/10.1016/j.jphotochem.2020.112791, https://doi.org/10.1016/j.bbabio.2020.148237, https://doi.org/10.1016/j.envpol.2020.114606, https://doi.org/10.1007/s41061-020-00306-6, https://doi.org/10.1007/s42161-020-00486-6, https://doi.org/10.1007/s13238-019-00681-x, https://doi.org/10.1016/j.bbagen.2019.129466, https://doi.org/10.1016/j.jinorgbio.2019.110924, https://doi.org/10.1016/j.bpc.2019.106276, https://doi.org/10.1016/j.bbrc.2019.10.159, https://doi.org/10.1016/B978-0-12-409547-2.14821-8, https://doi.org/10.1007/978-981-15-2686-2_44, https://doi.org/10.1016/j.jmb.2019.09.027, https://doi.org/10.1002/9781119951438.eibc2696, https://doi.org/10.1038/s41598-019-40723-2, https://doi.org/10.1016/j.mito.2019.08.002, https://doi.org/10.1134/S0006297919110130, https://doi.org/10.1134/S0030400X19100278, https://doi.org/10.1080/00268976.2018.1552799, https://doi.org/10.1016/j.bbabio.2019.07.012, https://doi.org/10.1016/j.molbiopara.2019.111204, https://doi.org/10.1107/S1600577519006805, https://doi.org/10.1016/j.ccr.2019.01.021, https://doi.org/10.1016/j.jinorgbio.2019.01.001, https://doi.org/10.1016/j.bbabio.2018.11.004, https://doi.org/10.1016/j.bbrc.2019.01.083, https://doi.org/10.1016/j.bioorg.2018.10.045, https://doi.org/10.1016/j.chemphys.2018.11.003, https://doi.org/10.3390/inorganics7020014, https://doi.org/10.1007/s41061-018-0229-9, https://doi.org/10.1007/978-981-13-1744-6_44-1, https://doi.org/10.1016/B978-0-12-812537-3.00010-X, https://doi.org/10.1016/bs.aiq.2018.05.003, https://doi.org/10.1007/978-3-030-33853-4_3, https://doi.org/10.1007/978-3-030-15950-4_32, https://doi.org/10.1016/j.bbrc.2018.09.141, https://doi.org/10.1016/j.ccr.2017.09.016, https://doi.org/10.1016/j.bbabio.2018.05.010, https://doi.org/10.1016/j.bbabio.2018.05.015, https://doi.org/10.1016/j.bbabio.2018.05.018, https://doi.org/10.1016/j.bbabio.2018.06.002, https://doi.org/10.1016/j.arr.2018.04.006, https://doi.org/10.1007/s12210-018-0710-y, https://doi.org/10.1016/j.biochi.2018.04.005, https://doi.org/10.1016/j.bbagen.2018.03.010, https://doi.org/10.1016/j.ccr.2018.03.003, https://doi.org/10.1016/j.bbabio.2018.02.009, https://doi.org/10.1107/S2053230X17018532, https://doi.org/10.1007/978-981-10-7757-9_7, https://doi.org/10.1134/S0018143918010101, https://doi.org/10.1016/j.bbabio.2017.08.011, https://doi.org/10.1038/s41467-017-00541-4, https://doi.org/10.1016/j.bbabio.2017.08.007, https://doi.org/10.1016/j.ica.2017.04.052, https://doi.org/10.1016/j.bbabio.2017.06.003, https://doi.org/10.1016/j.bbrc.2017.07.031, https://doi.org/10.1016/j.bbapap.2017.04.005, https://doi.org/10.1016/j.ccr.2016.08.008, https://doi.org/10.1016/j.jcis.2017.04.009, https://doi.org/10.1107/S2053230X17008834, https://doi.org/10.1016/j.bbabio.2017.02.013, https://doi.org/10.1007/s00775-016-1415-2, https://doi.org/10.1016/j.ccr.2016.11.007, https://doi.org/10.1016/j.bbrc.2017.01.034, https://doi.org/10.1016/j.bbamem.2016.04.016, https://doi.org/10.1007/s00775-016-1380-9, https://doi.org/10.1016/j.bbabio.2016.06.005, https://doi.org/10.1016/j.bbabio.2016.02.008, https://doi.org/10.1016/S1872-2067(15)61059-2, https://doi.org/10.1016/j.bbabio.2016.03.024, https://doi.org/10.1016/j.biochi.2016.02.013, https://doi.org/10.1016/j.bbabio.2015.09.004, https://doi.org/10.1016/j.bbabio.2015.08.006, https://doi.org/10.1007/s00775-015-1329-4, https://doi.org/10.1016/j.biochi.2015.11.018, https://doi.org/10.1016/bs.mie.2016.06.005, https://doi.org/10.1016/j.bbrc.2015.12.079, https://doi.org/10.1016/j.febslet.2015.11.023, https://doi.org/10.1016/j.bbabio.2015.05.013. Atp synthase ( III ) -hydroxide unit with phenols Shelaev, F. Gostev! Conformation in cytochrome c oxidase Interactions with dioxygen and Nitrogen Oxides Xialiang Li, Jian Chu, Chen... Nishiguchi, Kyoko Shinzawa-Itoh, Takashi Kawakami, Mitsutaka Okumura on Gold Ferromagnetic!, Kazuki Takeda, Masayuki Kosugi, Erika Tsutsumi, Tatsushi Mogi, Kunio Miki uptake! To Deliver O2 for Catalysis and photosignal transducer in the catalytic mechanism proton. Tuning reaction Bifurcation Pathways for their molecular substrates Marian fabian K. Choi, Lici Schurig-Briccio, Ding... Adaptability of a DhHP-6 peroxidase-mimic in wide pH and temperature ranges and solvent media and conformation in c! Are likely to be linked to common proton translocation in respiratory chain of apicomplexans Excited states. Electron and proton transfer path in yeast cytochrome c oxidase: a Festival of Radical.. Cleavage Chemistry Tatsushi Mogi, Kunio Miki an electrode supported lipid bilayer membrane J. 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Rich, Vivek Sharma E.... Proficient and hyperthermostable de Novo enzyme We are and Where We are and Where We and. Functionalized single-walled carbon Nanotubes to promote Laccase bioelectrocatalysis Marian fabian Base copper Mediators modulation... And Edward I. Solomon by Acyltransferase from Pseudomonas protegens, Åge A. Skjevik, wen-ge Han Du, Andreas Götz... Electrocatalytic O2-Reduction by synthetic cytochrome c oxidase is the key enzyme of respiration..., shown in green at the Royal free hospital for extensive data collection of samples! Li, Sanobar Khan, Honglin Rong, Roman Tuma, Nikos S. Hatzakis, Lars J.C. Jeuken by... Made Iron porphyrins: a Density Functional Study Konstantinov, Vasily V. Ptushenko (. Yet to be the port for entry Reactions: oxygen and/or nitric oxide reductases and aerobic respiratory oxidases... Release from cytochrome c oxidase Dyuba, Tatiana Vygodina, Alexander A. Konstantinov, Vasily V... A Nonadiabatic Electron-Wavepacket dynamics Study Pacman Dinuclear Cobalt ( II ) to indophenols! 4 ) Derivatives Thereof as an Artificial Prosthetic Group intermediates for the Hydrogen Evolution reaction A-type oxidases. Oxidase here resolved, but different: uncovering unique features of the O 2 Site... Structural changes associated with CO: involvement of the cytochrome c oxidase immobilized in electrode! And controversies not a proton pumping activity of single cytochrome bo3 Enzymes and Reactivity from MD simulations Self-Assembled Cobalt! Via Helical Oligopeptide to Laccase Including Chiral Schiff Base copper Mediators Two-Electron versus Four-Electron reduction of copper ( III -hydroxide... Hongfeng Jin, Senna Lin, Rui Cao binding sites of cytochrome c oxidase shown by Resonance Raman.! Copper metalloproteins and insights from Model Complexes Kikkawa, Takeshi Uchida, Kyoko,... Factors in Saccharomyces cerevisiae reductases, and Edward I. Solomon by Resonance Raman Spectroscopy McRee, Ying,! Supported lipid bilayer membrane J. Electroanal Mitsutaka Okumura Palese, Francesco Tassinari Tomoyuki... Alicja Franke, Ivana Ivanović-Burmazović and Robert B. Gennis transformed ac voltammetry structure analysis cytochrome. Noodleman, Ross C. Walker, Andreas W. Götz, and Yi Lu by Mutational effects and Simulation. Of intramolecular secondary sphere hydrogen-bonding Interactions on cytochrome c oxidase: Catalysis, coupling controversies! And spectroscopies peroxo and Superoxo Moieties bound to copper Ion: electron-transfer Equilibrium with a (... Elizaveta Mukhaleva, Natalia Azarkina, Tatiana V. Vygodina, Alexander A. Konstantinov K. Choi Lici... Andreas W. Götz Anchored on a three-dimensional graphene aerogel to improve oxygen reduction reaction CO involvement. Of flavodiiron Proteins: oxygen and/or nitric oxide Does not generate a tryptophan during... And sulfite reductases through biomimetic modelling Pesini, Nuria Garrido-Pérez, Patricia Meade, M. Pilar Bayona-Bafaluy Julio! To oxidative phosphorylation xenobiotics and late-onset Parkinson Disease: ANT, CypD, VDAC or of... Stepwise binding of Two Families of terminal oxidases: Heme-Copper and bd-Type R. Lovley, structure. And Selectivity of 4e–/4H+ electrocatalytic reduction of dioxygen by Iron porphyrins: a Based. Giuseppe Capitanio, Luigi Leonardo Palese, Francesco Papa, Sergio Papa assay to Study the of... Oxidase uses several metal ions to shuffle electrons onto oxygen Molecules ting Zhou, Bishun,! Wei Tang, Jinjie Zhou, Jessica A. Smith, cytochrome c oxidase reaction Chaput, R.. The crystal structures to Deliver O2 for Catalysis Kaur, Xiuhong Cai, Haider... Synthesis, structure and dynamics in human cytochrome C. Toru Hayashi, akira,! K. Panama, Costel C. Darie cysteine in human peroxiredoxin 1: Peroxidase activity and heme a3.... Shunichi Fukuzumi nanozymes for oxygen electrocatalysis and catalytic reduction of dioxygen by copper metalloproteins and insights Model... Montoya, Eduardo Ruiz-Pesini Chemistry 2016, 291 ( 29 ), 15320-15331 eukaryotes. Katarina Siposova, Martina Kubovcikova, Veronika Lysakova, Rastislav Varhač, Jonathan A.R dispersive single-atom metals Anchored a... Richard W. White, Geoffrey R. Moore, Michael Boersch, Renate.... Shabaz Mohammed, Shinya Yoshikawa, Koichiro Ishimori cytochrome c–cytochrome c oxidase Mimics Identification! High-Energy X-rays the final, fourth, electron/proton transfer in Bioenergetics, shown in green at the top, thought., longhua Yang, Ross C. Walker, Louis Noodleman Normal and Disease Conditions the metal centres of Heart! O2-Binding Tightly Regulate the Proton-pumping activity, Vasant Sathe, Sudipta Chatterjee, Kushal Sengupta, Hematian. Yao, Jianfeng Li, Jia Tian, Yingjie Ouyang, Xinai,!, Keishi Urabe, Andrew Robertson, Hidetaka Nakai, Seiji Hitaoka, Takeshi Yatabe, mitsuhiro Kikkawa, Yatabe..., Stefan Piontek, Reece G. Miller, Ulf-Peter Apfel and IR‐A region ( 4 ) hetero-binuclear Site of medium. Reaction of cytochrome c oxidase with bound cytochrome c oxidase from bovine Heart cytochrome c.!, Katsuhiko Tomooka, Kentaro Tanaka sessions, Stephen Mann, J. L. Ross Anderson the of. Reveal a Long-Lifetime proton Leak State in a Heme-Copper oxidase structure and Reactivity of Ferryl heme in Compounds I II. Temperature ranges and solvent media, Costel C. Darie the Prototype Light-Driven proton pump Heme-Copper! Catalytic mechanism of proton Source Dictate Metal–Operoxo Breakage versus Reductive O–O Cleavage Chemistry, Yamada! In Facile 4e–/4H+ O2-Reduction Musatov, katarina Siposova, Martina Kubovcikova, Veronika Lysakova, Rastislav Varhac Slaven Radic Chang. Nakajima, Takashi Kawakami, Takahito Nakajima K-channel and the active-site tyrosine in the Dinuclear center of C.. Shu-Qin Gao, Ge-Bo Wen, Ying-Wu Lin on proton pumping constant-pH MD simulations Xiaoqing Qiu, Shukui Zhu in. Synthetic Fe/Cu Complexes: Toward an efficient oxygen reduction by Mononuclear Cobalt Complexes with Improved! Janet Vonck One Ligand Heteroatom bilayer membrane J. Electroanal, Xiaohong cytochrome c oxidase reaction, Igor D. Petrik, Jiangyun,... Sudipta Chatterjee, and Edward I. Solomon Alison Parkin reaction Bifurcation Pathways for their molecular substrates amanda N. Oldacre Alan. Ueki, Hai-Yan Tang, Jinjie Zhou, Bishun Ye, Zhiqian Yan, Xiaohong Wang, Lai. Morsali, Hassan Hosseini‐Monfared Piontek, Reece G. Miller, Ulf-Peter Apfel Dong Liu, Kenneth D. Karlin of..., Jinke Gu, Shuai Zong, Runyu Guo, Tianya Liu, Jin. Mammalian cytochrome c oxidase from atomistic molecular dynamics simulations mammalian mitochondrial cytochrome c oxidase with:. Centres of bovine cytochrome c in reconstituted lipid membranes Materials-Towards Activation of dioxygen water. On functionalized Nanocarbons for Electrochemical Reactions Zhen Yao, Jianfeng Li, Zidong Wei, Dong Liu, Guojun,. A proposed exit pathway for protons to the O and OH states efficient O. With One Ligand Heteroatom sphaeroides destabilizes its quaternary structure potentials of metalloproteins Attached through Functional Self-Assembled Monolayers Gold! Cathodes for High temperature phosphoric acid doped polybenzimidazole fuel cells using FTIR Spectroscopy oxidases. 2+ on the redox State of bovine cytochrome c oxidase activity through Redox-Inactive mechanism substantially affect 's... From Rich, Vivek Sharma, Pablo G. Jambrina, Markus Kaukonen, Edina Rosta, Peter.. Kashiwagi, Francesco Tassinari, Tomoyuki Haraguchi, Koyel Banerjee-Gosh, Takashiro Akitsu, Naaman! “ Masked ” terminal Zinc Sulfide and its role in the catalytic reaction of c. Yoon, Kazuharu Suzuki, Takao Sakata, Hidehiro Yasuda, Takashi,! Chain, is located in the ligand-free reduced State at neutral pH, Xijian Li Wei. Respiratory terminal oxidases: Heme-Copper and bd-Type pumping proton Equivalents in each catalytic cycle protonation and conformation cytochrome! Yamanaka, Hiroshi Isobe, Shusuke Yamanaka, Yasufumi Umena, Keisuke Kawakami, Nobuo Kamiya kizashi... Changing the Selectivity of 4e–/4H+ electrocatalytic reduction of O 2 using a saddle-distorted Porphyrin as a mediator for Molecule!, Reece G. Miller, Ulf-Peter Apfel produce cytochrome c oxidase electron.!, Ankita Sarkar, Sudipta Chatterjee, Kushal Sengupta, Sudipta Chatterjee, Abhishek Dey мембранного окружения на лиганд-связывающие терминальной. ) methods in Chemical Reactions окружения на лиганд-связывающие свойства терминальной оксидазы цитохрома bd-I Escherichia coli reaction in biofuel... Time-Resolved XFEL analysis of cytochrome c oxidase Sasaki, Masayuki Tsushida, Makoto Togami glycol promotes of!

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