(2012) Respiratory Chains: Structures, Mechanisms and Energy Coupling. 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. Paween Mahinthichaichan, Robert B. Gennis, Emad Tajkhorshid. Angela Paulus, Carolin Werner, Bernd Ludwig, Simon de Vries. 2 oxidase. Andrey Musatov, Katarina Siposova, Martina Kubovcikova, Veronika Lysakova, Rastislav Varhac. ) porphyrin–porphyrin dyad. When the enzyme is not present, the reagent remains reduced and is colorless. c A question of flexibility in cytochrome c oxidase models. An Fe-based Model for Metabolism Linking between O 2 Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure. 2 Emi Aoki, Wataru Suzuki, Hiroaki Kotani, Tomoya Ishizuka, Hayato Sakai, Taku Hasobe, Takahiko Kojima. M. Adam, Gayan B. Wijeratne, Patrick J. Rogler, Daniel E. Diaz, David A. Quist, Jeffrey J. Liu. Sk Amanullah, Asmita Singha, Abhishek Dey. In: Edward H. Egelman, editor: Comprehensive Biophysics, Vol 8, Chapter 6, Bioenergetics (Stuart Ferguson, ed. Christopher J. Kingsbury, Mathias O. Senge. 3 CfbA promotes insertion of cobalt and nickel into ruffled tetrapyrroles Oxygen Reduction to Water by a Cofacial Dimer of Iron(III)-Porphyrin and Iron(III)-Phthalocyanine Linked through a Highly Flexible Fourfold Rotaxane. The redox-coupled proton-channel opening in cytochrome Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c. Toru Hayashi, Akira Yamaguchi, Kazuhito Hashimoto, Ryuhei Nakamura. Heme–Cu Binucleating Ligand Supports Heme/O2 and FeII–CuI/O2 Reactivity Providing High- and Low-Spin FeIII–Peroxo–CuII Complexes. Go Ueno, Atsuhiro Shimada, Eiki Yamashita, Kazuya Hasegawa, Takashi Kumasaka, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Tomitake Tsukihara, Masaki Yamamoto. Peroxo and Superoxo Moieties Bound to Copper Ion: Electron-Transfer Equilibrium with a Small Reorganization Energy. c Wen-Ge Han Du, Andreas W. Götz, and Louis Noodleman . 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. Michael Electron transfer is coupled to proton translocation across the membrane, resulting in a proton and charge gradient that is then employed by the FF-ATPase to synthesize ATP. Atsuhiro Shimada, Keita Hatano, Hitomi Tadehara, Naomine Yano, Kyoko Shinzawa-Itoh, Eiki Yamashita, Kazumasa Muramoto, Tomitake Tsukihara, Shinya Yoshikawa. [Jul 2013] Bruker alpha machine is installed at the Royal Free hospital for extensive data collection of urine samples. Cytochrome c oxidase is the key enzyme of cell respiration in all eukaryotes and many prokaryotes. 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. c Mechanistic dichotomies in redox reactions of mononuclear metal–oxygen intermediates. When present, the cytochrome c oxidase oxidizes the reagent (tetramethyl-p-phenylenediamine) to (indophenols) purple color end product. Suzanne M. Adam, Isaac Garcia-Bosch, Andrew W. Schaefer, Savita K. Sharma, Maxime A. Siegler, Edward I. Solomon, and Kenneth D. Karlin . 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 … Time-resolved studies of metalloproteins using X-ray free electron laser radiation at SACLA. 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 . Cytochrome c oxidase, the terminal enzyme in the respiratory chain, is located in the inner membrane of mitochondria and bacteria. It plays a vital role in enabling the cytochrome a 3 - Cu B binuclear center to accept four electrons in … An innovative in vitro assay to study the effects of aromatic pollutants on porphyrin systems. Attaching Cobalt Corroles onto Carbon Nanotubes: Verification of Four-Electron Oxygen Reduction by Mononuclear Cobalt Complexes with Significantly Improved Efficiency. Chen Li, Tatsuhito Nishiguchi, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Takashi Ogura, Satoru Nakashima. Courtney E. Elwell, Nicole L. Gagnon, Benjamin D. Neisen, Debanjan Dhar, Andrew D. Spaeth, Gereon M. Yee, and William B. Tolman . Xiuhong Cai, Kamran Haider, Jianxun Lu, Slaven Radic, Chang Yun Son, Qiang Cui, M.R. 72-93, Academic Press, Oxford). The oxidase test is used to identify bacteria that produce cytochrome c oxidase, an enzyme of the bacterial electron transport chain. Devika Channaveerappa, Brian K. Panama, Costel C. Darie. Same same, but different: Uncovering unique features of the mitochondrial respiratory chain of apicomplexans. oxidase utilizing high-energy X-rays. 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). A. Ehudin, Laura Senft, Alicja Franke, Ivana Ivanović-Burmazović. 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. Reversible dimerization of cytochrome c oxidase regulates mitochondrial respiration. and Maréchal, A. Effects of membrane curvature and pH on proton pumping activity of single cytochrome bo3 enzymes. Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli. [Nov 2013] We now have a newly refurbished spectroscopy lab. Connecting CuA with metal centers of heme a, heme a, CuB and Zn by pathways with hydrogen bond as the bridging element in cytochrome c oxidase. c 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. Wataru Sato, Seiji Hitaoka, Kaoru Inoue, Mizue Imai, Tomohide Saio, Takeshi Uchida, Kyoko Shinzawa-Itoh, Shinya Yoshikawa, Kazunari Yoshizawa, Koichiro Ishimori. Andrew W. Schaefer, Matthew T. Kieber-Emmons, Suzanne M. Adam, Kenneth D. Karlin, and Edward I. Solomon . Ilya P. Oleynikov, Natalia V. Azarkina, Tatiana V. Vygodina, Alexander A. Konstantinov. Biochimica et Biophysica Acta (BBA) - Bioenergetics. Construction and in vivo assembly of a catalytically proficient and hyperthermostable de novo enzyme. Cytochrome aa3 Oxygen Reductase Utilizes the Tunnel Observed in the Crystal Structures To Deliver O2 for Catalysis. Two copper atoms, shown in green at the top, are thought to be the port for entry. Water exit pathways and proton pumping mechanism in B-type cytochrome c oxidase from molecular dynamics simulations. Fangjia Luo, Kyoko Shinzawa-Itoh, Kaede Hagimoto, Atsuhiro Shimada, Satoru Shimada, Eiki Yamashita, Shinya Yoshikawa, Tomitake Tsukihara. Effect of Membrane Environment on the Ligand-Binding Properties of the Terminal Oxidase Cytochrome bd-I from Escherichia coli. in bovine cytochrome 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. 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. 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. Dinuclear Complexes Formed by Hydrogen Bonds: Synthesis, Structure and Magnetic and Electrochemical Properties. Efficient Solar-Assisted O Influence of Ligand Architecture in Tuning Reaction Bifurcation Pathways for Chlorite Oxidation by Non-Heme Iron Complexes. a Chemical Biology of H2S Signaling through Persulfidation. c The radical is re-reduced by the third electron/proton transfer in the P→F step. 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. Yuta Watanabe, Koichiro Ishimori, Takeshi Uchida. Satoru Shimada, Kyoko Shinzawa‐Itoh, Junpei Baba, Shimpei Aoe, Atsuhiro Shimada, Eiki Yamashita, Jiyoung Kang, Masaru Tateno, Shinya Yoshikawa, Tomitake Tsukihara. -reduction Site of Bovine Heart Cytochrome Biochimica et Biophysica Acta (BBA) - Bioenergetics 1988 , 932 , 277-286. Wataru Sato, Takeshi Uchida, Tomohide Saio, Koichiro Ishimori. The proton pumping bo oxidase from Vitreoscilla. Jianshe Huang, Qingqing Lu, Xiao Ma, Xiurong Yang. Pauline Vorburger, Mamadou Lo, Sylvie Choua, Maxime Bernard, Frédéric Melin, Nesrine Oueslati, Corinne Boudon, Mourad Elhabiri, Jennifer A. Wytko, Petra Hellwig, Jean Weiss. The oxygen reduction reaction cycle of cytochrome c oxidase (taken from Rich, P.R. c c Cytochrome containing organisms produce an intracellular oxidase enzyme. It is also considered as the photoacceptor and photosignal transducer in the region of visible and IR‐A region (4). A Cu and Fe dual-atom nanozyme mimicking cytochrome c oxidase to boost the oxygen reduction reaction† Cheng Du , ‡ ad Yijing Gao , ‡ b Hengquan Chen , c Ping Li , ad Shuyun Zhu , e Jianguo Wang , * b Qinggang He * c and Wei Chen * ad Hydrosulfide complexes of the transition elements: diverse roles in bioinorganic, cluster, coordination, and organometallic chemistry. The mechanism of coupling between oxido-reduction and proton translocation in respiratory chain enzymes. 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). Insights into proton translocation in cbb 3 oxidase from MD simulations. Zuozhong Liang, Hong-Yan Wang, Haoquan Zheng, Wei Zhang, Rui Cao. 8.3 Complex IV activity assay: Energetic Mechanism of Cytochrome c -Cytochrome c Oxidase Electron Transfer Complex Formation under Turnover Conditions Revealed by Mutational Effects and Docking Simulation. 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 . • Kumarswamy R, Chandna S (February 2009). Structure Effects of Metal Corroles on Energy-Related Small Molecule Activation Reactions. Chemical Transformations in Confined Space of Coordination Architectures. Pseudomonas aeruginosa overexpression system of nitric oxide reductase for in vivo and in vitro mutational analyses. 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. Characterisation of the Cyanate Inhibited State of Cytochrome c Oxidase. Rhodobacter sphaeroides Snapshot of an oxygen intermediate in the catalytic reaction of cytochrome Methanosarcina acetivorans Takehiro Ohta, Perumandla Nagaraju, Jin-Gang Liu, Takashi Ogura, Yoshinori Naruta. Roles of the indole ring of Trp396 covalently bound with the imidazole ring of His398 coordinated to type I copper in bilirubin oxidase. For cytochrome c oxidase, the overall reaction is: 4 ferrocyt c + 4H + N + 4H + N + O 2 ==> 4 ferricyt c + + 2H 2 O + 4H + P. Since cytochrome c is in the P-phase, 8 charges are transfered from N- to P-phase per oxygen consumed. i Crystal Structure of an Active Form of Monomeric Cytochrome c Oxidase from Bovine Heart. Melanie Cytochrome c oxidase reaction cycle The oxygen reduction reaction cycle of cytochrome c oxidase (taken from Rich, P.R. Mechanism of Biocatalytic Friedel–Crafts Acylation by Acyltransferase from Pseudomonas protegens. 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. Method for Enzyme Design with Genetically Encoded Unnatural Amino Acids. Changqing Du, Yingzheng Weng, Jiangjie Lou, Guangzhong Zeng, Xiaowei Liu, Hongfeng Jin, Senna Lin, Lijiang Tang. Calcium ions inhibit reduction of heme oxidase. To Conserve Energy from Extracellular Electron Transfer. c The catalytic mechanism of CcO has yet to be resolved, but several mechanisms have been proposed. Crossref | ISI Google Scholar; 23. Michihiro Suga, Atsuhiro Shimada, Fusamichi Akita, Jian-Ren Shen, Takehiko Tosha, Hiroshi Sugimoto. Damián Alvarez-Paggi, Luciana Hannibal, María A. Castro, Santiago Oviedo-Rouco, Veronica Demicheli, Veronica Tórtora, Florencia Tomasina, Rafael Radi, and Daniel H. Murgida . Bionic design of cytochrome c oxidase-like single-atom nanozymes for oxygen reduction reaction in enzymatic biofuel cells. Douglas C. Wallace, Marie T. Lott, Vincent Procaccio. Synthesis of a “Masked” Terminal Zinc Sulfide and Its Reactivity with Brønsted and Lewis Acids. Mixture. Mathias O. Senge, Stuart A. MacGowan, Jessica M. O'Brien. Naomine Yano, Kazumasa Muramoto, Atsuhiro Shimada, Shuhei Takemura, Junpei Baba, Hidenori Fujisawa, Masao Mochizuki, Kyoko Shinzawa-Itoh, Eiki Yamashita, Tomitake Tsukihara, Shinya Yoshikawa. Rabia Ramzan, Annika Rhiel, Petra Weber, Bernhard Kadenbach, Sebastian Vogt. Mitochondrion. It catalyses the reduction of dioxygen to water and pumps an additional proton across the membrane for each proton consumed in the reaction. Structure Changes Induced by O2-binding Tightly Regulate the Proton-pumping of Cytochrome c Oxidase. Proceedings of the National Academy of Sciences. Hendrik Mohrmann, Jovan Dragelj, Federico Baserga, Ernst-Walter Knapp, Sven T. Stripp, Joachim Heberle. The cytochrome ba3 oxidase from Thermus thermophilus does not generate a tryptophan radical during turnover: Implications for the mechanism of proton pumping. 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. –cytochrome Performance of a time-resolved IR facility for assessment of protonation states and polarity changes in carboxyl groups in a large membrane protein, mammalian cytochrome c oxidase, under turnover conditions in a sub-millisecond time resolution. Miguel Á. Baeza Cinco, Guang Wu, Nikolas Kaltsoyannis, Trevor W. Hayton. Functional adlayers on Au electrodes: some recent applications in hydrogen evolution and oxygen reduction. Michael Kizashi Yamaguchi, Hiroshi Isobe, Mitsuo Shoji, Koichi Miyagawa, Shusuke Yamanaka, Takashi Kawakami, Takahito Nakajima. oxidase. Design and fine-tuning redox potentials of metalloproteins involved in electron transfer in bioenergetics. doi:10.1016/j.mito.2008.10.003. A Self-Assembled Cofacial Cobalt Porphyrin Prism for Oxygen Reduction Catalysis. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. Librarians & Account Managers. 3 Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry. O ), pp. First demonstration of phosphate enhanced atomically dispersed bimetallic FeCu catalysts as Pt-free cathodes for high temperature phosphoric acid doped polybenzimidazole fuel cells. Electron Transport Mechanism of Mitochondrial Respiratory Megacomplex Structure of bovine cytochrome Copper Enzymes Involved in Multi-Electron Processes. Reaction of cytochrome c oxidase with CO: involvement of the invisible copper. Abstract. Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins. c The dual function of flavodiiron proteins: oxygen and/or nitric oxide reductases. The cellular membrane as a mediator for small molecule interaction with membrane proteins. Interaction of Cytochrome C Oxidase with Steroid Hormones. Saccharomyces cerevisiae. Scienze Fisiche e Naturali. Kyoko SHINZAWA-ITOH, Kazumasa MURAMOTO. Heme isomers substantially affect heme's electronic structure and function. c Explaining leak states in the proton pump of heme-copper oxidases observed in single-molecule experiments. A Fusion of Biomimetic Fuel and Solar Cells Based on Hydrogenase, Photosystem II, and Cytochrome c Oxidase. Spontaneous Reduction of Copper(II) to Copper(I) at Solid–Liquid Interface. A nanosecond time-resolved XFEL analysis of structural changes associated with CO release from cytochrome c oxidase. Mitochondrial Structure and Bioenergetics in Normal and Disease Conditions. Activation of dioxygen by copper metalloproteins and insights from model complexes. Both reactions lead to formation of derivatives responsible of the mitochondrial nitrosative stress observed in different pathophysiological conditions, including main neurodegenerations [ 2 – 6 ]. Jia Meng, Haitao Lei, Xialiang Li, Jing Qi, Wei Zhang. oxidase. The reaction mechanism in both directions is complex. JBIC Journal of Biological Inorganic Chemistry. CuB2+ Dinuclear Center of the Resting Oxidized as-Isolated Cytochrome c Oxidase: A Density Functional Study. Rhoten, J.D. Haitao Lei, Xialiang Li, Jia Meng, Haoquan Zheng, Wei Zhang. Heme: From quantum spin crossover to oxygen manager of life. Critical Aspects of Heme–Peroxo–Cu Complex Structure and Nature of Proton Source Dictate Metal–Operoxo Breakage versus Reductive O–O Cleavage Chemistry. oxidase—DFT calculated properties compared to structures and spectroscopies. Idlir Liko, Matteo T. Degiacomi, Shabaz Mohammed, Shinya Yoshikawa, Carla Schmidt, Carol V. Robinson. moieties anchored on a three-dimensional graphene aerogel to improve oxygen reduction catalytic performance. Lindsay JG, Owen CS, Wilson DF. Vivek Sharma, Pablo G. Jambrina, Markus Kaukonen, Edina Rosta, Peter R. Rich. Ashta C. Ghosh, Carole Duboc, Marcello Gennari. Katarina Kopcova, Ludmila Blascakova, Tibor Kozar, Daniel Jancura. Ru(II)-diimine functionalized metalloproteins: From electron transfer studies to light-driven biocatalysis. Femtosecond Absorption Spectroscopy of Reduced and Oxidized Forms of Cytochrome c Oxidase: Excited States and Relaxation Processes in Heme a and a3 Centers. )-hydroxide unit with phenols. Using Tryptophan Mutants To Probe the Structural and Functional Status of BsSCO, a Copper Binding, Cytochrome c Oxidase Assembly Protein from Bacillus subtilis. Campos, António M. Baptista, Cláudio M. Soares. Click on the image for a bigger version (150K). [Oct 2013] See our latest mini review on the metal centres of bovine cytochrome c oxidase here. 2 Wataru Sato, Seiji Hitaoka, Takeshi Uchida, Kyoko Shinzawa-Itoh, Kazunari Yoshizawa, Shinya Yoshikawa, Koichiro Ishimori. Copper-Promoted Functionalization of Organic Molecules: from Biologically Relevant Cu/O2 Model Systems to Organometallic Transformations. Влияние мембранного окружения на лиганд-связывающие свойства терминальной оксидазы цитохрома bd-I Escherichia coli. Effect of Ca 2+ on the redox potential of heme a in cytochrome c oxidase. The Journal of Physical Chemistry Letters. The Mg2+-containing Water Cluster of Mammalian Cytochrome c Oxidase Collects Four Pumping Proton Equivalents in Each Catalytic Cycle. Nitrite modulates aminoglycoside tolerance by inhibiting cytochrome heme-copper oxidase in bacteria. Constantinos Koutsoupakis, Tewfik Soulimane. Molecular understanding of heteronuclear active sites in heme–copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling. I2III2IV2. 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. Monomeric structure of an active form of bovine cytochrome From Enzymes to Functional Materials-Towards Activation of Small Molecules. Mass Spectrometry Based Comparative Proteomics Using One Dimensional and Two Dimensional SDS-PAGE of Rat Atria Induced with Obstructive Sleep Apnea. Satomi Niwa, Kazuki Takeda, Masayuki Kosugi, Erika Tsutsumi, Tatsushi Mogi, Kunio Miki. Recent Developments in Metalloporphyrin Electrocatalysts for Reduction of Small Molecules: Strategies for Managing Electron and Proton Transfer Reactions. Kunishige Kataoka, Takahiro Ito, Yoko Okuda, Yoko Sakai, Satoshi Yamashita, Takeshi Sakurai. c Tatiana V. Vygodina, Olga P. Kaminskaya, Alexander A. Konstantinov, Vasily V. Ptushenko. Transient-state studies of the reaction with oxygen have led to the proposal of a … Cytochrome c oxidase uses several metal ions to shuffle electrons onto oxygen molecules. Michael D. Pluth, Zachary J. Tonzetich. On the role of subunit M in cytochrome cbb 3 oxidase. Possibility of the right-opened Mn-oxo intermediate (R-oxo(4444)) among all nine intermediates in the S3 state of the oxygen-evolving complex of photosystem II revealed by large-scale QM/MM calculations. Porphyrinoid–Cyclodextrin Assemblies in Biomedical Research: An Update. Osmotic pressure effects identify dehydration upon cytochrome c–cytochrome c oxidase complex formation contributing to a specific electron pathway formation. X Crystal structure of heme A synthase from Coupling between protonation and conformation in cytochrome c oxidase: Insights from constant-pH MD simulations. Joana S. Sousa, Edoardo D’Imprima, Janet Vonck. Modulation of the electron-proton coupling at cytochrome a by the ligation of the oxidized catalytic center in bovine cytochrome c oxidase. Comparison of redox and ligand binding behaviour of yeast and bovine cytochrome c oxidases using FTIR spectroscopy. Chem., 534 (2002), pp. c. Shunichi Fukuzumi, Kyung-Bin Cho, Yong-Min Lee, Seungwoo Hong, Wonwoo Nam. iii Factors Determining the Rate and Selectivity of 4e–/4H+ Electrocatalytic Reduction of Dioxygen by Iron Porphyrin Complexes. Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a “Bridging Peroxo” Intermediate Involved in Facile 4e–/4H+ O2-Reduction. He Zhang, Liang Huang, Jinxing Chen, Ling Liu, Xinyang Zhu, Weiwei Wu, Shaojun Dong. Frauke Möller, Stefan Piontek, Reece G. Miller, Ulf-Peter Apfel. Worrall. Mitochondrial Respiratory Chain Complexes. Giuseppe Capitanio, Luigi Leonardo Palese, Francesco Papa, Sergio Papa. Biochemical and Biophysical Research Communications. Sylvia K. Choi, Lici Schurig-Briccio, Ziqiao Ding, Sangjin Hong, Chang Sun, and Robert B. Gennis . Cytochrome c (Cyt c) plays a crucial role in this energy production by means of the electron transport chain (ETC), transferring electrons between complexes ΙΙΙ (cytochrome bc 1) and ΙV (cytochrome c oxidase, CcO). 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