{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,4,17]],"date-time":"2023-04-17T02:17:05Z","timestamp":1681697825428},"reference-count":63,"publisher":"Portland Press Ltd.","issue":"5","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2013,10,1]]},"abstract":"<jats:p>Assignments of IR bands of reduced minus oxidized IR difference spectra of bovine and related cytochrome c oxidases are reviewed and their linkages to specific metal centres are assessed. To aid this, redox-poised difference spectra in the presence of cyanide or carbon monoxide are presented. These ligands fix the redox states of either haem a3 alone or haem a3 and CuB respectively, while allowing redox cycling of the remaining centres.<\/jats:p>","DOI":"10.1042\/bst20130087","type":"journal-article","created":{"date-parts":[[2013,9,23]],"date-time":"2013-09-23T15:37:32Z","timestamp":1379950652000},"page":"1242-1248","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":8,"title":["IR signatures of the metal centres of bovine cytochrome <i>c<\/i> oxidase: assignments and redox-linkage"],"prefix":"10.1042","volume":"41","author":[{"given":"Raksha","family":"Dodia","sequence":"first","affiliation":[{"name":"Institute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Amandine","family":"Mar\u00e9chal","sequence":"additional","affiliation":[{"name":"Institute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Simona","family":"Bettini","sequence":"additional","affiliation":[{"name":"Department of Biological and Environmental Sciences and Technologies, DISTEBA, University of Salento, Via per Arnesano, I-73100 Lecce, Italy"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masayo","family":"Iwaki","sequence":"additional","affiliation":[{"name":"Department of Frontier Materials, Nagoya Institute of Technology, Gokiso Nagoya 466-8555, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Peter\u00a0R.","family":"Rich","sequence":"additional","affiliation":[{"name":"Institute of Structural and Molecular Biology, University College London, Gower Street, London WC1E 6BT, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2013,9,23]]},"reference":[{"key":"2021111720272920000_B1","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1042\/bse0470001","article-title":"The mitochondrial respiratory chain","volume":"47","author":"Rich","year":"2010","journal-title":"Essays Biochem."},{"key":"2021111720272920000_B2","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/B978-0-12-374920-8.00806-7","article-title":"Electron transfer chains: structures, mechanisms and energy coupling","volume-title":"Comprehensive Biophysics","author":"Rich","year":"2012"},{"key":"2021111720272920000_B3","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/j.bbabio.2011.12.012","article-title":"Structural studies on bovine heart cytochrome c oxidase","volume":"1817","author":"Yoshikawa","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B4","doi-asserted-by":"crossref","first-page":"20130813","DOI":"10.1098\/rsif.2013.0183","article-title":"Functions of the hydrophilic channels in protonmotive cytochrome c oxidase","volume":"10","author":"Rich","year":"2013","journal-title":"J. R. Soc. Interface"},{"key":"2021111720272920000_B5","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/j.bbabio.2004.01.007","article-title":"FTIR studies of internal proton transfer reactions linked to inter-heme electron transfer in bovine cytochrome c oxidase","volume":"1655","author":"McMahon","year":"2004","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B6","doi-asserted-by":"crossref","first-page":"13195","DOI":"10.1021\/bi971091o","article-title":"Fourier transform infrared evidence for connectivity between CuB and glutamic acid 286 in cytochrome bo3 from E. coli","volume":"36","author":"Puustinen","year":"1997","journal-title":"Biochemistry"},{"key":"2021111720272920000_B7","doi-asserted-by":"crossref","first-page":"7209","DOI":"10.1021\/ja021302z","article-title":"FTIR detection of protonation\/deprotonation of key carboxyl side chains caused by redox change of the CuA-heme a moiety and ligand dissociation from the heme a3-CuB center of bovine heart cytochrome c oxidase","volume":"125","author":"Okuno","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"2021111720272920000_B8","doi-asserted-by":"crossref","first-page":"7565","DOI":"10.1021\/bi990225q","article-title":"Time-resolved FT-IR studies on the CO adduct of Paracoccus denitrificans cytochrome c oxidase: comparison of the fully reduced and the mixed valence form","volume":"38","author":"Rost","year":"1999","journal-title":"Biochemistry"},{"key":"2021111720272920000_B9","doi-asserted-by":"crossref","first-page":"6441","DOI":"10.1021\/bi0027332","article-title":"FTIR studies of the CO and cyanide compounds of fully reduced bovine cytochrome c oxidase","volume":"40","author":"Rich","year":"2001","journal-title":"Biochemistry"},{"key":"2021111720272920000_B10","doi-asserted-by":"crossref","first-page":"2048","DOI":"10.1021\/bi981859k","article-title":"Electron transfer induces side-chain conformational changes of glutamate-286 from cytochrome bo3","volume":"38","author":"L\u00fcbben","year":"1999","journal-title":"Biochemistry"},{"key":"2021111720272920000_B11","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1093\/oxfordjournals.jbchem.a022423","article-title":"Effects of subunit I mutations on redox-linked conformational changes of the Escherichia coli bo-type ubiquinol oxidase revealed by Fourier-transform infrared spectroscopy","volume":"126","author":"Yamazaki","year":"1999","journal-title":"J. Biochem. (Tokyo)"},{"key":"2021111720272920000_B12","doi-asserted-by":"crossref","first-page":"9116","DOI":"10.1021\/bi012056r","article-title":"Vibrational modes of tyrosine in cytochrome c oxidase from Paracoccus denitrificans: FTIR and electrochemical studies on Tyr-D4-labeled and on Tyr280His and Tyr35Phe mutant enzymes","volume":"41","author":"Hellwig","year":"2002","journal-title":"Biochemistry"},{"key":"2021111720272920000_B13","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/0014-5793(96)00342-0","article-title":"Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy","volume":"385","author":"Hellwig","year":"1996","journal-title":"FEBS Lett."},{"key":"2021111720272920000_B14","doi-asserted-by":"crossref","first-page":"7390","DOI":"10.1021\/bi9725576","article-title":"Involvement of glutamic acid 278 in the redox reaction of the cytochrome c oxidase from Paracoccus denitrificans investigated by FTIR spectroscopy","volume":"37","author":"Hellwig","year":"1998","journal-title":"Biochemistry"},{"key":"2021111720272920000_B15","doi-asserted-by":"crossref","first-page":"7400","DOI":"10.1021\/bi9731697","article-title":"Redox dependent changes at the heme propionates in cytochrome c oxidase from Paracoccus denitrificans: direct evidence from FTIR difference spectroscopy in combination with heme propionate 13C labelling","volume":"37","author":"Behr","year":"1998","journal-title":"Biochemistry"},{"key":"2021111720272920000_B16","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/0968-0004(93)90186-Q","article-title":"Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms","volume":"18","author":"M\u00e4ntele","year":"1993","journal-title":"Trends Biochem. Sci."},{"key":"2021111720272920000_B17","doi-asserted-by":"crossref","first-page":"565","DOI":"10.1111\/j.1432-1033.1990.tb15338.x","article-title":"Redox-linked conformational changes in proteins detected by a combination of IR spectroscopy and protein electrochemistry: evaluation of the technique with cytochrome c","volume":"187","author":"Moss","year":"1990","journal-title":"Eur. J. Biochem."},{"key":"2021111720272920000_B18","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0304-4157(99)00004-0","article-title":"Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes","volume":"1422","author":"Goormaghtigh","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B19","doi-asserted-by":"crossref","first-page":"588","DOI":"10.1366\/0003702963905907","article-title":"ATR\/FT-IR difference spectroscopy of biological matter with microsecond time resolution","volume":"50","author":"Heberle","year":"1996","journal-title":"Appl. Spectrosc."},{"key":"2021111720272920000_B20","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1039\/b702328f","article-title":"Methods to probe protein transitions with ATR infrared spectroscopy","volume":"3","author":"Rich","year":"2007","journal-title":"Mol. Biosys."},{"key":"2021111720272920000_B21","doi-asserted-by":"crossref","first-page":"2386","DOI":"10.1021\/ja039320j","article-title":"Direct detection of formate ligation in cytochrome c oxidase by ATR-FTIR spectroscopy","volume":"126","author":"Iwaki","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"2021111720272920000_B22","doi-asserted-by":"crossref","first-page":"5802","DOI":"10.1021\/ja4005706","article-title":"Structural changes in cytochrome c oxidase induced by binding of sodium and calcium ions: an ATR-FTIR study","volume":"135","author":"Mar\u00e9chal","year":"2013","journal-title":"J. Am. Chem. Soc."},{"key":"2021111720272920000_B23","doi-asserted-by":"crossref","first-page":"116","DOI":"10.1016\/S0005-2728(02)00265-7","article-title":"ATR-FTIR difference spectroscopy of the PM intermediate of bovine cytochrome c oxidase","volume":"1555","author":"Iwaki","year":"2002","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B24","doi-asserted-by":"crossref","first-page":"10873","DOI":"10.1021\/bi061114b","article-title":"Structural and chemical changes of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase revealed by IR spectroscopy with labeled tyrosines and histidines","volume":"45","author":"Iwaki","year":"2006","journal-title":"Biochemistry"},{"key":"2021111720272920000_B25","doi-asserted-by":"crossref","first-page":"8715","DOI":"10.1073\/pnas.1530408100","article-title":"Direct observation of protonation reactions during the catalytic cycle of cytochrome c oxidase","volume":"100","author":"Nyquist","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111720272920000_B26","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0014-5793(01)02769-7","article-title":"Perfusion-induced redox differences in cytochrome c oxidase: ATR\/FT-IR spectroscopy","volume":"505","author":"Nyquist","year":"2001","journal-title":"FEBS Lett."},{"key":"2021111720272920000_B27","doi-asserted-by":"crossref","first-page":"13141","DOI":"10.1021\/bi701614w","article-title":"Time-resolved ATR-FTIR spectroscopy of the oxygen reaction in the D124N mutant of cytochrome c oxidase from Paracoccus denitrificans","volume":"46","author":"Gorbikova","year":"2007","journal-title":"Biochemistry"},{"key":"2021111720272920000_B28","doi-asserted-by":"crossref","first-page":"8634","DOI":"10.1073\/pnas.1019419108","article-title":"Water molecule reorganization in cytochrome c oxidase revealed by FTIR spectroscopy","volume":"108","author":"Mar\u00e9chal","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111720272920000_B29","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0079-6107(00)00021-3","article-title":"The infrared absorption of amino acid side chains","volume":"74","author":"Barth","year":"2000","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"2021111720272920000_B30","first-page":"314","article-title":"Infrared protein spectroscopy as a tool to study protonation reactions within proteins","volume-title":"Biophysical and Structural Aspects of Bioenergetics","author":"Rich","year":"2005"},{"key":"2021111720272920000_B31","doi-asserted-by":"crossref","first-page":"1685","DOI":"10.1021\/bi982282+","article-title":"Electrochemical and ultraviolet\/visible\/infrared spectroscopic analysis of heme a and a3 redox reactions in the cytochrome c oxidase from Paracoccus denitrificans: separation of heme a and a3 contributions and assignment of vibrational modes","volume":"38","author":"Hellwig","year":"1999","journal-title":"Biochemistry"},{"key":"2021111720272920000_B32","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1021\/bi0109717","article-title":"Attenuated total reflection Fourier transform infrared studies of redox changes in bovine cytochrome c oxidase: resolution of the redox Fourier transform infrared difference spectrum of heme a3","volume":"41","author":"Rich","year":"2002","journal-title":"Biochemistry"},{"key":"2021111720272920000_B33","doi-asserted-by":"crossref","first-page":"5641","DOI":"10.1021\/bi060257v","article-title":"Redox titration of all electron carriers of cytochrome c oxidase by Fourier transform infrared spectroscopy","volume":"45","author":"Gorbikova","year":"2006","journal-title":"Biochemistry"},{"key":"2021111720272920000_B34","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/S0006-3495(86)83500-7","article-title":"Resonance Raman spectral isolation of the a and a3 chromophores in cytochrome oxidase","volume":"50","author":"Argade","year":"1986","journal-title":"Biophys. J."},{"key":"2021111720272920000_B35","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.ab.2009.06.035","article-title":"Identification of heme propionate vibrational modes in the resonance Raman spectra of cytochrome c oxidase","volume":"394","author":"Egawa","year":"2009","journal-title":"Anal. Biochem."},{"key":"2021111720272920000_B36","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/0005-2728(90)90022-V","article-title":"The effect of pH on redox titrations of haem a in cyanide-liganded cytochrome-c oxidase: experimental and modelling studies","volume":"1015","author":"Moody","year":"1990","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B37","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/0014-5793(74)81058-6","article-title":"Reaction of cytochrome c oxidase with CO: involvement of the invisible copper","volume":"48","author":"Lindsay","year":"1974","journal-title":"FEBS Lett."},{"key":"2021111720272920000_B38","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1098\/rspb.1940.0040","article-title":"Succinic dehydrogenase\u2013cytochrome system of cells: intracellular respiratory system catalysing aerobic oxidation of succinic acid","volume":"129","author":"Keilin","year":"1940","journal-title":"Proc. R. Soc. London Ser. B"},{"key":"2021111720272920000_B39","doi-asserted-by":"crossref","first-page":"6375","DOI":"10.1016\/S0021-9258(19)44703-0","article-title":"Studies on cytochrome oxidase VIII: preparation and some properties of cardiac cytochrome oxidase","volume":"247","author":"Kuboyama","year":"1972","journal-title":"J. Biol. Chem."},{"key":"2021111720272920000_B40","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/S0005-2728(05)80204-X","article-title":"Characterisation of \u2018fast\u2019 and \u2018slow\u2019 forms of bovine heart cytochrome c oxidase","volume":"1059","author":"Moody","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B41","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1007\/BF00762850","article-title":"Probing heart cytochrome c oxidase structure and function by infrared spectroscopy","volume":"25","author":"Caughey","year":"1993","journal-title":"J. Bioenerg. Biomemb."},{"key":"2021111720272920000_B42","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0014-5793(99)01133-3","article-title":"Similarities and dissimilarities in the structure\u2013function relation between the cytochrome c oxidase from bovine heart and from Paracoccus denitrificans as revealed by FT-IR difference spectroscopy","volume":"458","author":"Hellwig","year":"1999","journal-title":"FEBS Lett."},{"key":"2021111720272920000_B43","doi-asserted-by":"crossref","first-page":"8809","DOI":"10.1021\/bi034522d","article-title":"ATR-FTIR spectroscopy of the PM and F intermediates of bovine and Paracoccus denitrificans cytochrome c oxidase","volume":"42","author":"Iwaki","year":"2003","journal-title":"Biochemistry"},{"key":"2021111720272920000_B44","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1021\/bi00052a022","article-title":"Fourier-transform infrared study of cyanide binding to the Fea3-CuB binuclear site of bovine heart cytochrome c oxidase: implication of the redox-linked conformational change at the binuclear site","volume":"32","author":"Tsubaki","year":"1993","journal-title":"Biochemistry"},{"key":"2021111720272920000_B45","doi-asserted-by":"crossref","first-page":"4270","DOI":"10.1074\/jbc.270.9.4270","article-title":"Effects of overall oxidation state on infrared spectra of heme a3 cyanide in bovine heart cytochrome c oxidase: evidence of novel mechanistic roles for CuB","volume":"270","author":"Yoshikawa","year":"1995","journal-title":"J. Biol. Chem."},{"key":"2021111720272920000_B46","doi-asserted-by":"crossref","first-page":"1356","DOI":"10.1021\/bi991504g","article-title":"Functional properties of the heme propionates in cytochrome c oxidase from Paracoccus denitrificans: evidence from FTIR difference spectroscopy and site-directed mutagenesis","volume":"39","author":"Behr","year":"2000","journal-title":"Biochemistry"},{"key":"2021111720272920000_B47","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1016\/j.bbabio.2008.04.035","article-title":"Carboxyl group functions in the heme-copper oxidases: information from mid-IR vibrational spectroscopy","volume":"1777","author":"Rich","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B48","doi-asserted-by":"crossref","first-page":"7959","DOI":"10.1021\/bi052183d","article-title":"Calculated proton uptake on anaerobic reduction of cytochrome c oxidase: is the reaction electroneutral?","volume":"45","author":"Song","year":"2006","journal-title":"Biochemistry"},{"key":"2021111720272920000_B49","doi-asserted-by":"crossref","first-page":"14370","DOI":"10.1021\/bi048545j","article-title":"ATR-FTIR spectroscopy and isotope labelling of the PM intermediate of Paracoccus denitrificans cytochrome c oxidase","volume":"43","author":"Iwaki","year":"2004","journal-title":"Biochemistry"},{"key":"2021111720272920000_B50","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1111\/j.1749-6632.1973.tb43217.x","article-title":"Infrared spectroscopy of porphyrins","volume":"206","author":"Alben","year":"1973","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"2021111720272920000_B51","doi-asserted-by":"crossref","first-page":"1340","DOI":"10.1021\/ja00982a011","article-title":"The infrared spectra of metalloproteins (4000\u2013160 cm\u22121)","volume":"89","author":"Boucher","year":"1967","journal-title":"J. Am. Chem. Soc."},{"key":"2021111720272920000_B52","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1016\/B978-0-12-220103-5.50014-3","article-title":"Infrared spectroscopy of porphyrins","volume-title":"the Porphyrins","author":"Alben","year":"1978"},{"key":"2021111720272920000_B53","doi-asserted-by":"crossref","first-page":"4526","DOI":"10.1063\/1.436450","article-title":"Resonance Raman spectra of octaethylporphyrinato-Ni(II) and meso-deuterated and 15N substituted derivatives. II. A normal coordinate analysis","volume":"69","author":"Abe","year":"1978","journal-title":"J. Chem. Phys."},{"key":"2021111720272920000_B54","doi-asserted-by":"crossref","first-page":"11460","DOI":"10.1021\/bi00161a026","article-title":"Molecular changes following oxidoreduction of cytochrome b559 characterized by Fourier transform infrared difference spectroscopy and electron paramagnetic resonance: photooxidation in photosystem II and electrochemistry of isolated cytochrome b559 and iron protoporphyrin IX\u2013bisimidazole model compounds","volume":"31","author":"Berthomieu","year":"1992","journal-title":"Biochemistry"},{"key":"2021111720272920000_B55","doi-asserted-by":"crossref","first-page":"3377","DOI":"10.1021\/jp012251f","article-title":"Ab initio density functional theory calculations and vibrational analysis of zinc-bound 4-methylimidazole as a model of a histidine ligand in metalloenzymes","volume":"106","author":"Hasegawa","year":"2002","journal-title":"J. Phys. Chem. A"},{"key":"2021111720272920000_B56","doi-asserted-by":"crossref","first-page":"4253","DOI":"10.1021\/jp000157d","article-title":"Vibrational spectra and ab initio DFT calculations of 4-methylimidazole and its different protonation forms: infrared and Raman markers of the protonation state of a histidine side chain","volume":"104","author":"Hasegawa","year":"2000","journal-title":"J. Phys. Chem. B"},{"key":"2021111720272920000_B57","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/0005-2728(74)90038-3","article-title":"Haem\u2013haem interactions in cytochrome aa3 during the anaerobic\u2013aerobic transition","volume":"357","author":"Nicholls","year":"1974","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B58","doi-asserted-by":"crossref","first-page":"1723","DOI":"10.1126\/science.280.5370.1723","article-title":"Redox-coupled crystal structural changes in bovine heart cytochrome c oxidase","volume":"280","author":"Yoshikawa","year":"1998","journal-title":"Science"},{"key":"2021111720272920000_B59","doi-asserted-by":"crossref","first-page":"15304","DOI":"10.1073\/pnas.2635097100","article-title":"The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process","volume":"100","author":"Tsukihara","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111720272920000_B60","doi-asserted-by":"crossref","first-page":"4200","DOI":"10.1073\/pnas.0611627104","article-title":"The proton pumping pathway of bovine heart cytochrome c oxidase","volume":"104","author":"Shimokata","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111720272920000_B61","doi-asserted-by":"crossref","first-page":"S102","DOI":"10.1016\/j.bbabio.2012.06.276","article-title":"Functions of the hydrophilic channels of mitochondrial forms of cytochrome oxidase from studies of yeast mutants","volume":"1817","author":"Rich","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"2021111720272920000_B62","doi-asserted-by":"crossref","first-page":"7062","DOI":"10.1021\/cr1002003","article-title":"Proton-coupled electron transfer in cytochrome oxidase","volume":"110","author":"Kaila","year":"2010","journal-title":"Chem. Rev."},{"key":"2021111720272920000_B63","doi-asserted-by":"crossref","first-page":"1136","DOI":"10.1126\/science.272.5265.1136","article-title":"The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 \u00c5","volume":"272","author":"Tsukihara","year":"1996","journal-title":"Science"}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/41\/5\/1242\/484215\/bst0411242.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/41\/5\/1242\/484215\/bst0411242.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,18]],"date-time":"2021-11-18T00:25:38Z","timestamp":1637195138000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/41\/5\/1242\/66247\/IR-signatures-of-the-metal-centres-of-bovine"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,9,23]]},"references-count":63,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2013,9,23]]},"published-print":{"date-parts":[[2013,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bst20130087","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,9,23]]}}}