Structure of bovine cytochrome Paween Mahinthichaichan, Robert B. Gennis. [Oct 2013] See our latest mini review on the metal centres of bovine cytochrome c oxidase here. 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). Development of broken-symmetry (BS) methods in chemical reactions.,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, Dwaipayan Dutta Gupta, Dandamudi Usharani, Shyamalava Mazumdar. Journal of Photochemistry and Photobiology A: Chemistry. In: Edward H. Egelman, editor: Comprehensive Biophysics, Vol 8, Chapter 6, Bioenergetics (Stuart Ferguson, ed. FEBS Lett 48: 45–49, 1974. Courtney E. Elwell, Nicole L. Gagnon, Benjamin D. Neisen, Debanjan Dhar, Andrew D. Spaeth, Gereon M. Yee, and William B. Tolman . The cellular membrane as a mediator for small molecule interaction with membrane proteins. Ashta C. Ghosh, Carole Duboc, Marcello Gennari. On the basis of these results a minimum reaction mechanism i … Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. O-oxidation. 2 Heme: From quantum spin crossover to oxygen manager of life. Divya Kaur, Xiuhong Cai, Umesh Khaniya, Yingying Zhang, Junjun Mao, Manoj Mandal, Marilyn Gunner. From Enzymes to Functional Materials-Towards Activation of Small Molecules. Zachary Thammavongsy, Ian P. Mercer, Jenny Y. Yang. Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli. 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. c. Shunichi Fukuzumi, Kyung-Bin Cho, Yong-Min Lee, Seungwoo Hong, Wonwoo Nam. Biochemical and Biophysical Research Communications. It plays a vital role in enabling the cytochrome a 3 - Cu B binuclear center to accept four electrons in … An Fe-based Model for Metabolism Linking between O 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. 2 The effect of the trans axial ligand of cobalt corroles on water oxidation activity in neutral aqueous solutions. Atsuhiro Shimada, Keita Hatano, Hitomi Tadehara, Naomine Yano, Kyoko Shinzawa-Itoh, Eiki Yamashita, Kazumasa Muramoto, Tomitake Tsukihara, Shinya Yoshikawa. Interaction of Cytochrome C Oxidase with Steroid Hormones. 2 Cytochrome c oxidase inhibition by calcium at physiological ionic composition of the medium: Implications for physiological significance of the effect. Single Enzyme Experiments Reveal a Long-Lifetime Proton Leak State in a Heme-Copper Oxidase. Changqing Du, Yingzheng Weng, Jiangjie Lou, Guangzhong Zeng, Xiaowei Liu, Hongfeng Jin, Senna Lin, Lijiang Tang. Sylvia K. Choi, Lici Schurig-Briccio, Ziqiao Ding, Sangjin Hong, Chang Sun, and Robert B. Gennis . Settling the Long-Standing Debate on the Proton Storage Site of the Prototype Light-Driven Proton Pump Bacteriorhodopsin. Naumann. ~ 15 min: Fix … Attaching Cobalt Corroles onto Carbon Nanotubes: Verification of Four-Electron Oxygen Reduction by Mononuclear Cobalt Complexes with Significantly Improved Efficiency. in reconstituted lipid membranes. Probing the nitrite and nitric oxide reductase activity of cbb Célia V. Romão, João B. Vicente, Patrícia T. Borges, Carlos Frazão, Miguel Teixeira. It catalyzes the reduction of dioxygen to water, a process involving the addition of four electrons and four protons. Mitsuhiro Kikkawa, Takeshi Yatabe, Takahiro Matsumoto, Ki-Seok Yoon, Kazuharu Suzuki, Takao Enomoto, Kenji Kaneko, Seiji Ogo. Each of the four electron transfers into the BNC is accompanied by uptake of a charge-compensating substrate proton. [Jul 2013] Bruker alpha machine is installed at the Royal Free hospital for extensive data collection of urine samples. Femtosecond absorption spectroscopy of cytochrome c oxidase: Excited electronic states and relaxation processes in heme a and heme a3 centers. Theoretical and computational investigations of geometrical, electronic and spin structures of the CaMn A decomposes in microseconds to P, breaking the O=O bond to form a ferryl heme (Fe4+=O2-), CuB2+OH- and a neutral tyrosine radical (●OTyr). Tatiana V. Vygodina, Olga P. Kaminskaya, Alexander A. Konstantinov, Vasily V. Ptushenko. 143-150 Chemical Biology of H2S Signaling through Persulfidation. Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function. The Glynn Laboratory of Bioenergetics at UCL, University College London, Gower Street, London, WC1E 6BT Tel: +44 (0) 20 7679 2000. Giuseppe Capitanio, Luigi Leonardo Palese, Francesco Papa, Sergio Papa. 8.2.2 Prepare 120 µL of diluted Cytochrome c per reaction. Heme–Cu Binucleating Ligand Supports Heme/O2 and FeII–CuI/O2 Reactivity Providing High- and Low-Spin FeIII–Peroxo–CuII Complexes. Zachary Gordon, Michael J. Drummond, Ellen M. Matson, Justin A. Bogart, Eric J. Schelter, Richard L. Lord, and Alison R. Fout . Insights into proton translocation in cbb 3 oxidase from MD simulations. X Mengqiu Li, Sune K. Jørgensen, Duncan G. G. McMillan, Łukasz Krzemiński, Nikolaos N. Daskalakis, Riitta H. Partanen, Marijonas Tutkus, Roman Tuma, Dimitrios Stamou, Nikos S. Hatzakis, and Lars J. C. Jeuken . Reactivity of the copper( Roles of the indole ring of Trp396 covalently bound with the imidazole ring of His398 coordinated to type I copper in bilirubin oxidase. Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics. Tracing the Pathways of Waters and Protons in Photosystem II and Cytochrome c Oxidase. Constantinos Koutsoupakis, Tewfik Soulimane. The reaction mechanism in both directions is complex. Reduction Using a Cofacial Iron Porphyrin Dimer Catalyst Integrated into a p-CuBi Dan Lou, Xi-Chun Liu, Xiao-Juan Wang, Shu-Qin Gao, Ge-Bo Wen, Ying-Wu Lin. Fine Tuning of Functional Features of the CuA Site by Loop-Directed Mutagenesis. Jing Yu, Pin Chen, Jun Yang, Xiaoqing Qiu, Guohong Qiu, Shukui Zhu. International Journal of Molecular Sciences. 2 Nozomi Mihara, Yasuyuki Yamada, Hikaru Takaya, Yasutaka Kitagawa, Shin Aoyama, Kazunobu Igawa, Katsuhiko Tomooka, Kentaro Tanaka. Louis Noodleman, Wen-Ge Han Du, Duncan McRee, Ying Chen, Teffanie Goh, Andreas W. Götz. Multifunctional Cytochrome c: Learning New Tricks from an Old Dog. 4 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. 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. c Functional adlayers on Au electrodes: some recent applications in hydrogen evolution and oxygen reduction. JBIC Journal of Biological Inorganic Chemistry. 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. Lisi Xie, Jia Tian, Yingjie Ouyang, Xinai Guo, Weian Zhang, Ulf‐Peter Apfel, Wei Zhang, Rui Cao. Calcium ions inhibit reduction of heme Sergey A. Siletsky, Ilya Belevich, Nikolai P. Belevich, Tewfik Soulimane, Mårten Wikström. Crystallographic studies of cytochrome c oxidase show an unusual post-translational modification, linking C6 of Tyr (244) and the ε-N of His (240) (bovine enzyme numbering). Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry. First demonstration of phosphate enhanced atomically dispersed bimetallic FeCu catalysts as Pt-free cathodes for high temperature phosphoric acid doped polybenzimidazole fuel cells. On the role of subunit M in cytochrome cbb 3 oxidase. Influence of Ligand Architecture in Tuning Reaction Bifurcation Pathways for Chlorite Oxidation by Non-Heme Iron Complexes. Cytochrome c oxidase uses several metal ions to shuffle electrons onto oxygen molecules. Michihiro Suga, Atsuhiro Shimada, Fusamichi Akita, Jian-Ren Shen, Takehiko Tosha, Hiroshi Sugimoto. ), pp. 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. Cytochrome Zuozhong Liang, Hong-Yan Wang, Haoquan Zheng, Wei Zhang, Rui Cao. Zaki N. Zahran, Eman A. Mohamed, Ashraf Abdel Haleem, Yoshinori Naruta. c Samir Chattopadhyay, Ankita Sarkar, Sudipta Chatterjee, Abhishek Dey. Chemical Transformations in Confined Space of Coordination Architectures. Structure and Function of Respiratory Chain. catalytic intermediates Cytochrome c oxidase (C c O), a member of the oxygen reductase family of enzymes, is the terminal enzyme of the electron transfer … O A. Sofia F. Oliveira, Sara R.R. Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins. Water‐Soluble Polymers with Appending Porphyrins as Bioinspired Catalysts for the Hydrogen Evolution Reaction. 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.  oxidase reveals a novel protein–protein interaction mode. Development of de Novo Copper Nitrite Reductases: Where We Are and Where We Need To Go. Find more information about Crossref citation counts. Stone, Matthew D. Liptak. 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. Deciphering a 20-Year-Old Conundrum: The Mechanisms of Reduction by the Water/Amine/SmI B )-hydroxide unit with phenols. Sudipta Chatterjee, Kushal Sengupta, Biswajit Mondal, Subal Dey, and Abhishek Dey . Quan Lam, Mallory Kato, Lionel Cheruzel. Electron Transport Mechanism of Mitochondrial Respiratory Megacomplex Elisa Andresen, Edgar Peiter, Hendrik Küpper. Uranium inhibits mammalian mitochondrial cytochrome c oxidase and ATP synthase. Uncovering proteomics changes of Penicillium expansum spores in response to decanal treatment by iTRAQ. The role of the K-channel and the active-site tyrosine in the catalytic mechanism of cytochrome c oxidase. the Altmetric Attention Score and how the score is calculated. Xiuhong Cai, Kamran Haider, Jianxun Lu, Slaven Radic, Chang Yun Son, Qiang Cui, M.R. Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. 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. Isobaric tags for relative and absolute quantitation‑based proteomics reveals potential novel biomarkers for the early diagnosis of acute myocardial infarction within 3�h. c Synthesis of a “Masked” Terminal Zinc Sulfide and Its Reactivity with Brønsted and Lewis Acids. Wataru Sato, Seiji Hitaoka, Kaoru Inoue, Mizue Imai, Tomohide Saio, Takeshi Uchida, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Kazunari Yoshizawa, Koichiro Ishimori. Andrey Musatov, Katarina Siposova, Martina Kubovcikova, Veronika Lysakova, Rastislav Varhac. Arch Biochem Biophys 169: 492–505, 1975. Proteo-lipobeads to encapsulate cytochrome c oxidase from Paracoccus denitrificans. A broken-symmetry density functional study of structures, energies, and protonation states along the catalytic O–O bond cleavage pathway in ba Radicals in Action: A Festival of Radical Transformations. Suzanne M. Adam, Isaac Garcia-Bosch, Andrew W. Schaefer, Savita K. Sharma, Maxime A. Siegler, Edward I. Solomon, and Kenneth D. Karlin . Stepwise Binding of Two Azide Ions to the O Fabian Kruse, Anh Duc Nguyen, Jovan Dragelj, Ramona Schlesinger, Joachim Heberle, Maria Andrea Mroginski, Inez M. Weidinger. The Journal of Physical Chemistry Letters. S. Safarian, A. Hahn, D. J. Wei Zhang, Wenzhen Lai, and Rui Cao . Factors Determining the Rate and Selectivity of 4e–/4H+ Electrocatalytic Reduction of Dioxygen by Iron Porphyrin Complexes. Naomine Yano, Kazumasa Muramoto, Atsuhiro Shimada, Shuhei Takemura, Junpei Baba, Hidenori Fujisawa, Masao Mochizuki, Kyoko Shinzawa-Itoh, Eiki Yamashita, Tomitake Tsukihara, Shinya Yoshikawa. c A common coupling mechanism for A-type heme-copper oxidases from bacteria to mitochondria. Mitsuo Shoji, Hiroshi Isobe, Koichi Miyagawa, Kizashi Yamaguchi. Frauke Möller, Stefan Piontek, Reece G. Miller, Ulf-Peter Apfel. Electrocatalytic reduction of Molecular Oxygen with a Copper (II) Coordination Polymer. M.C. 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. Mengqiu Li, Sanobar Khan, Honglin Rong, Roman Tuma, Nikos S. Hatzakis, Lars J.C. Jeuken. Chen Li, Tatsuhito Nishiguchi, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Takashi Ogura, Satoru Nakashima. Shina Hussain, Diann Andrews, and Bruce C. Hill . 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. Andrej Musatov, Rastislav Varhač, Jonathan P. Hosler, Erik Sedlák. When present, the cytochrome c oxidase oxidizes the reagent (tetramethyl-p-phenylenediamine) to (indophenols) purple color end product. Campos, António M. Baptista, Cláudio M. Soares. Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c. Toru Hayashi, Akira Yamaguchi, Kazuhito Hashimoto, Ryuhei Nakamura. Energetic Mechanism of Cytochrome c-Cytochrome c Oxidase Electron Transfer Complex Formation under Turnover Conditions Revealed by Mutational Effects and Docking Simulation. Mass Spectrometry Based Comparative Proteomics Using One Dimensional and Two Dimensional SDS-PAGE of Rat Atria Induced with Obstructive Sleep Apnea. Mechanisms of Two-Electron versus Four-Electron Reduction of Dioxygen Catalyzed by Earth-Abundant Metal Complexes. Atsuhiro Shimada, Yuki Etoh, Rika Kitoh-Fujisawa, Ai Sasaki, Kyoko Shinzawa-Itoh, Takeshi Hiromoto, Eiki Yamashita, Kazumasa Muramoto, Tomitake Tsukihara, Shinya Yoshikawa. Devika Channaveerappa, Brian K. Panama, Costel C. Darie. Crystal structure of CO-bound cytochrome Atomistic insights into cardiolipin binding sites of cytochrome c oxidase. 9 (1): 1–8. Emi Aoki, Wataru Suzuki, Hiroaki Kotani, Tomoya Ishizuka, Hayato Sakai, Taku Hasobe, Takahiko Kojima. Amanda N. Oldacre, Alan E. Friedman, and Timothy R. Cook . The mechanism of coupling between oxido-reduction and proton translocation in respiratory chain enzymes. Kumpei Kashiwagi, Francesco Tassinari, Tomoyuki Haraguchi, Koyel Banerjee-Gosh, Takashiro Akitsu, Ron Naaman. Mohammad Ali Kamyabi, Fatemeh Soleymani‐Bonoti, Leila Taheri, Ahmad Morsali, Hassan Hosseini‐Monfared. Shunichi Fukuzumi, Yong-Min Lee, Wonwoo Nam. Alexander Wolf, Jovan Dragelj, Juliane Wonneberg, Johannes Stellmacher, Jens Balke, Anna Lena Woelke, Milan Hodoscek, Ernst Walter Knapp, Ulrike Alexiev. Haitao Lei, Xialiang Li, Jia Meng, Haoquan Zheng, Wei Zhang. Dinuclear Complexes Formed by Hydrogen Bonds: Synthesis, Structure and Magnetic and Electrochemical Properties. in vitro. a Theory of chemical bonds in metalloenzymes XXII: a concerted bond-switching mechanism for the oxygen–oxygen bond formation coupled with one electron transfer for water oxidation in the oxygen-evolving complex of photosystem II. oxidase. Hyun Kim, Savita K. Sharma, Andrew W. Schaefer, Edward I. Solomon. Artem V. Dyuba, Tatiana Vygodina, Natalia Azarkina, Alexander A. Konstantinov. Yang Yu, Chang Cui, Xiaohong Liu, Igor D. Petrik, Jiangyun Wang, and Yi Lu . c Michael i Cytochrome aa3 Oxygen Reductase Utilizes the Tunnel Observed in the Crystal Structures To Deliver O2 for Catalysis. To Conserve Energy from Extracellular Electron Transfer. Lindsay JG, Owen CS, Wilson DF. It catalyses the reduction of dioxygen to water and pumps an additional proton across the membrane for each proton consumed in the reaction. Catarina A. Carvalheda, Andrei V. Pisliakov. Network analysis of a proposed exit pathway for protons to the P-side of cytochrome c oxidase. Jianshe Huang, Qingqing Lu, Xiao Ma, Xiurong Yang. Debanjan Dhar, Gereon M. Yee, Todd F. Markle, James M. Mayer, William B. Tolman. Sessions, Stephen Mann, J. L. Ross Anderson. Gunner. Discrete Ligand Binding and Electron Transfer Properties of ba3-Cytochrome c Oxidase from Thermus thermophilus: Evolutionary Adaption to Low Oxygen and High Temperature Environments. [Nov 2013] We now have a newly refurbished spectroscopy lab. Dawn E. Holmes, Toshiyuki Ueki, Hai-Yan Tang, Jinjie Zhou, Jessica A. Smith, Gina Chaput, Derek R. Lovley, . Activity adaptability of a DhHP-6 peroxidase-mimic in wide pH and temperature ranges and solvent media. 4 Phenol-Induced O–O Bond Cleavage in a Low-Spin Heme–Peroxo–Copper Complex: Implications for O2 Reduction in Heme–Copper Oxidases. Go Ueno, Atsuhiro Shimada, Eiki Yamashita, Kazuya Hasegawa, Takashi Kumasaka, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Tomitake Tsukihara, Masaki Yamamoto. CfbA promotes insertion of cobalt and nickel into ruffled tetrapyrroles 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. 3 oxidase from atomistic molecular dynamics simulations. Worrall. Prakash Chandra Mondal, Claudio Fontanesi. Prenatal exposure to oxidative phosphorylation xenobiotics and late-onset Parkinson disease. The secondary coordination sphere and axial ligand effects on oxygen reduction reaction by iron porphyrins: a DFT computational study. M. Adam, Gayan B. Wijeratne, Patrick J. Rogler, Daniel E. Diaz, David A. Quist, Jeffrey J. Liu. A Membrane-Bound Cytochrome Enables Sudipta Chatterjee, Kushal Sengupta, Shabnam Hematian, Kenneth D. Karlin, and Abhishek Dey . Jin-Cheng Li, Zidong Wei, Dong Liu, Dan Du, Yuehe Lin, Minhua Shao. Michael D. Pluth, Zachary J. Tonzetich. Femtosecond Absorption Spectroscopy of Reduced and Oxidized Forms of Cytochrome c Oxidase: Excited States and Relaxation Processes in Heme a and a3 Centers. c Efficient photocatalytic proton-coupled electron-transfer reduction of O Changing the Selectivity of O2 Reduction Catalysis with One Ligand Heteroatom. Tatiana V. Vygodina, Elizaveta Mukhaleva, Natalia V. Azarkina, Alexander A. Konstantinov. 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.

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