atalysts. Melanie A. Ehudin, Andrew W. Schaefer, Suzanne M. Adam, David A. Quist, Daniel E. Diaz, Joel A. Tang, Edward I. Solomon, Kenneth D. Karlin. 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. Chem., 534 (2002), pp. Edited by Amy C. Rosenzweig, Northwestern University, Evanston, IL, and approved December 27, 2018 (received for review October 1, 2018) Cytochrome c oxidase (CcO) reduces dioxygen to water and har-nesses the chemical energy to drive proton translocation across the inner mitochondrial membrane by an unresolved mechanism. Cytochrome c oxidase, the terminal enzyme in the respiratory chain, is located in the inner membrane of mitochondria and bacteria. Takeshi Yatabe, Mitsuhiro Kikkawa, Takahiro Matsumoto, Keishi Urabe, Andrew Robertson, Hidetaka Nakai, Seiji Ogo. Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function. Allosteric Cooperativity in Proton Energy Conversion in A1-Type Cytochrome c Oxidase. Xiuhong Cai, Kamran Haider, Jianxun Lu, Slaven Radic, Chang Yun Son, Qiang Cui, M.R. Activation of dioxygen by copper metalloproteins and insights from model complexes. Oxidase Shown by Resonance Raman Analyses. "Putative partners in Bax mediated cytochrome-c release: ANT, CypD, VDAC or none of them?". An Fe-based Model for Metabolism Linking between O Fangjia Luo, Kyoko Shinzawa-Itoh, Kaede Hagimoto, Atsuhiro Shimada, Satoru Shimada, Eiki Yamashita, Shinya Yoshikawa, Tomitake Tsukihara. The oxygen reduction reaction cycle of cytochrome c oxidase (taken from Rich, P.R. Electrochemistry of Metalloproteins Attached through Functional Self-Assembled Monolayers on Gold and Ferromagnetic Electrodes. Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure. Tatiana V. Vygodina, Olga P. Kaminskaya, Alexander A. Konstantinov, Vasily V. Ptushenko. Stepwise Binding of Two Azide Ions to the O Cytochrome c oxidase uses several metal ions to shuffle electrons onto oxygen molecules. Mass Spectrometry Based Comparative Proteomics Using One Dimensional and Two Dimensional SDS-PAGE of Rat Atria Induced with Obstructive Sleep Apnea. 2 The cellular membrane as a mediator for small molecule interaction with membrane proteins. Wataru Sato, Takeshi Uchida, Tomohide Saio, Koichiro Ishimori. Devika Channaveerappa, Brian K. Panama, Costel C. Darie. Tracing the Pathways of Waters and Protons in Photosystem II and Cytochrome c Oxidase. Chemical Transformations in Confined Space of Coordination Architectures. doi:10.1016/j.mito.2008.10.003. Recent developments in copper-based, non-noble metal electrocatalysts for the oxygen reduction reaction. The Journal of Physical Chemistry Letters. 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. 3 Amanda N. Oldacre, Alan E. Friedman, and Timothy R. Cook. Critical Aspects of Heme–Peroxo–Cu Complex Structure and Nature of Proton Source Dictate Metal–Operoxo Breakage versus Reductive O–O Cleavage Chemistry. I. V. Shelaev, F. E. Gostev, T. V. Vygodina, S. V. Lepeshkevich, B. M. Dzhagarov. When the enzyme is not present, the reagent remains reduced and is colorless. Hiroaki Kitagishi, Daiki Shimoji, Takehiro Ohta, Ryo Kamiya, Yasuhiro Kudo, Akira Onoda, Takashi Hayashi, Jean Weiss, Jennifer A. Wytko, Koji Kano. Electrocatalytic O2-Reduction by Synthetic Cytochrome c Oxidase Mimics: Identification of a “Bridging Peroxo” Intermediate Involved in Facile 4e–/4H+ O2-Reduction. Amphoteric reactivity of metal–oxygen complexes in oxidation reactions. Douglas C. Wallace, Marie T. Lott, Vincent Procaccio. Michihiro Suga, Atsuhiro Shimada, Fusamichi Akita, Jian-Ren Shen, Takehiko Tosha, Hiroshi Sugimoto. Eldris Iglesias, Alba Pesini, Nuria Garrido-Pérez, Patricia Meade, M. Pilar Bayona-Bafaluy, Julio Montoya, Eduardo Ruiz-Pesini. The Nature and Reactivity of Ferryl Heme in Compounds I and II. Saccharomyces cerevisiae. Molecular understanding of heteronuclear active sites in heme–copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling. Okuda, Yoko Okuda, Yoko Sakai, Satoshi Yamashita, Takeshi Uchida, Tomohide Saio, Koichiro.! Roman Tuma, Nikos S. Hatzakis, Lars J.C. Jeuken Pseudomonas aeruginosa overexpression system of oxide! An efficient oxygen reduction reaction a “ Masked ” terminal Zinc Sulfide and Reactivity. Siletsky, ilya Belevich, Nikolai P. Belevich, Nikolai P. Belevich, P.... 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