<h1>Chan, Sunney</h1>
<h2>Combined from <a href="https://authors.library.caltech.edu">CaltechAUTHORS</a></h2>
<ul>
<li>Chan, Sunney I. and Wang, Vincent C.-C., el al. (2022) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20220708-259535200">Methane oxidation by the copper methane monooxygenase: Before and after the cryogenic electron microscopy structure of particulate methane monooxygenase from Methylococcus capsulatus (Bath)</a>; Journal of the Chinese Chemical Society; <a href="https://doi.org/10.1002/jccs.202200166">10.1002/jccs.202200166</a></li>
<li>Lu, Yu-Jhang and Hung, Mu-Cheng, el al. (2019) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20190417-075957631">PmoB subunit of particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath): The Cu^I sponge and its function</a>; Journal of Inorganic Biochemistry; Vol. 196; Art. No. 110691; <a href="https://doi.org/10.1016/j.jinorgbio.2019.04.005">10.1016/j.jinorgbio.2019.04.005</a></li>
<li>Chen, Nai-Chi and Yoshimura, Masato, el al. (2019) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20190301-081007422">The atomic structures of shrimp nodaviruses reveal new dimeric spike structures and particle polymorphism</a>; Communications Biology; Vol. 2; Art. No. 72; PMCID PMC6382870; <a href="https://doi.org/10.1038/s42003-019-0311-z">10.1038/s42003-019-0311-z</a></li>
<li>Guan, Hong-Hsiang and Hsieh, Yin-Cheng, el al. (2018) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20181016-085612513">Structural insights into the electron/proton transfer pathways in the quinol:fumarate reductase from Desulfovibrio gigas</a>; Scientific Reports; Vol. 8; Art. No. 14935; PMCID PMC6175931; <a href="https://doi.org/10.1038/s41598-018-33193-5">10.1038/s41598-018-33193-5</a></li>
<li>Wang, Vincent C.-C. and Maji, Suman, el al. (2017) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170221-133527458">Alkane Oxidation: Methane Monooxygenases, Related Enzymes, and Their Biomimetics</a>; Chemical Reviews; Vol. 117; No. 13; 8574-8621; <a href="https://doi.org/10.1021/acs.chemrev.6b00624">10.1021/acs.chemrev.6b00624</a></li>
<li>Pham, Minh D. and Lin, Ya-Ping, el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150824-122929840">Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene</a>; Biochimica et Biophysica Acta - Proteins and Proteomics; Vol. 1854; No. 12; 1842-1852; <a href="https://doi.org/10.1016/j.bbapap.2015.08.004">10.1016/j.bbapap.2015.08.004</a></li>
<li>Chen, Nai-Chi and Yoshimura, Masato, el al. (2015) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20151103-082920090">Crystal Structures of a Piscine Betanodavirus: Mechanisms of Capsid Assembly and Viral Infection</a>; PLoS Pathogens; Vol. 11; No. 10; Art. No. e1005203; PMCID PMC4619592; <a href="https://doi.org/10.1371/journal.ppat.1005203">10.1371/journal.ppat.1005203</a></li>
<li>Hu, Cheng and Chan, Sunney I., el al. (2014) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20230411-407202000.2">Metalloprotein design using genetic code expansion</a>; Chemical Society Reviews; Vol. 43; No. 18; 6498-6510; <a href="https://doi.org/10.1039/c4cs00018h">10.1039/c4cs00018h</a></li>
<li>Chen, C. and Hsieh, Y., el al. (2014) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20140425-084531804">Crystal Structure of Dihydropyrimidinase from Tetraodon nigroviridis with Lysine Carboxylation: Metal Requirement for Post-translational Modification and Function</a>; Journal of Biological Inorganic Chemistry; Vol. 19; No. S1; S91; <a href="https://doi.org/10.1007/s00775-014-1095-8">10.1007/s00775-014-1095-8</a></li>
<li>Hsieh, Yin-Cheng and Chen, Mei-Chun, el al. (2013) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20140214-093236082">Crystal Structures of Vertebrate Dihydropyrimidinase and Complexes from Tetraodon nigroviridis with Lysine Carbamylation</a>; Journal of Biological Chemistry; Vol. 288; No. 42; 30645-30658; PMCID PMC3798535; <a href="https://doi.org/10.1074/jbc.M113.496778">10.1074/jbc.M113.496778</a></li>
<li>Fang, Jou-Yin and Chiang, Yuan-Lan, el al. (2011) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20110621-085539646">Crystallization of Adenylylsulfate Reductase from Desulfovibrio gigas: A Strategy Based on Controlled Protein Oligomerization</a>; Crystal Growth and Design; Vol. 11; No. 6; 2127-2134; <a href="https://doi.org/10.1021/cg1013818">10.1021/cg1013818</a></li>
<li>Chan, Sunney I. and Nguyen, H.-Hoa T., el al. (2011) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20110603-135022605">Overexpression and Purification of the Particulate Methane Monooxygenase from Methylococcus capsulatus (Bath)</a>; ISBN 9780123869050; Methods in Methane Metabolism. Part B, Methanotrophy; 177-193; <a href="https://doi.org/10.1016/B978-0-12-386905-0.00012-7">10.1016/B978-0-12-386905-0.00012-7</a></li>
<li>Hsieh, Yin-Cheng and Liu, Ming-Yih, el al. (2010) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20110104-081227286">Structural insights into the enzyme catalysis from comparison of three forms of dissimilatory sulphite reductase from Desulfovibrio gigas</a>; Molecular Microbiology; Vol. 78; No. 5; 1101-1116; <a href="https://doi.org/10.1111/j.1365-2958.2010.07390.x">10.1111/j.1365-2958.2010.07390.x</a></li>
<li>Chan, Sunney I. (2010) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20100610-081630636">Proton pumping in cytochrome c oxidase: The coupling between proton and electron gating</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 107; No. 19; 8505-8506; PMCID PMC2889352; <a href="https://doi.org/10.1073/pnas.1004050107">10.1073/pnas.1004050107</a></li>
<li>Chan, Sunney I. (2009) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20090813-122034630">A physical chemist's expedition to explore the world of membrane proteins</a>; Annual Reviews of Biophysics; Vol. 38; 1-27; <a href="https://doi.org/10.1146/annurev.biophys.050708.133713">10.1146/annurev.biophys.050708.133713</a></li>
<li>Chan, Sunney I. and Yu, Steve S.-F. (2008) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170131-071607269">Controlled Oxidation of Hydrocarbons by the Membrane-Bound Methane Monooxygenase: The Case for a Tricopper Cluster</a>; Accounts of Chemical Research; Vol. 41; No. 8; 969-979; <a href="https://doi.org/10.1021/ar700277n">10.1021/ar700277n</a></li>
<li>Chen, Peter P.-Y. and Yang, Richard B.-G., el al. (2007) <a href="https://resolver.caltech.edu/CaltechAUTHORS:CHEpnas07b">Facile O-atom insertion into C-C and C-H bonds by a trinuclear copper complex designed to harness a singlet oxene</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 104; No. 37; 14570-14575; PMCID PMC1976241; <a href="https://doi.org/10.1073/pnas.0707119104">10.1073/pnas.0707119104</a></li>
<li>Pavlova, Svetlana V. and To, Hing Lun, el al. (2006) <a href="https://resolver.caltech.edu/CaltechAUTHORS:PAVdt06">Synthesis, structure and dioxygen reactivity of a bis(µ-iodo)dicopper(I) complex supported by the [N-(3,5-di-tert-butyl-2-hydroxybenzyl)-N,N-di-(2-pyridylmethyl)]amine ligand</a>; Dalton Transactions; Vol. 2006; No. 18; 2232-2243; <a href="https://doi.org/10.1039/b513898a">10.1039/b513898a</a></li>
<li>Chen, Rita P.-Y. and Huang, Joseph J.-T., el al. (2004) <a href="https://resolver.caltech.edu/CaltechAUTHORS:CHEpnas04">Measuring the refolding of β-sheets with different turn sequences on a nanosecond time scale</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 101; No. 19; 7305-7310; PMCID PMC409914; <a href="https://doi.org/10.1073/pnas.0304922101">10.1073/pnas.0304922101</a></li>
<li>Chan, Sunney I. and Chen, Kelvin H.-C., el al. (2004) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170131-140941315">Toward Delineating the Structure and Function of the Particulate Methane Monooxygenase from Methanotrophic Bacteria</a>; Biochemistry; Vol. 43; No. 15; 4421-4430; <a href="https://doi.org/10.1021/bi0497603">10.1021/bi0497603</a></li>
<li>Pavlova, Svetlana V. and Chen, Kelvin H.-C., el al. (2004) <a href="https://resolver.caltech.edu/CaltechAUTHORS:PAVdt04">Spectroscopic characterization of the oxo-transfer reaction from a bis(µ-oxo)dicopper(III) complex to triphenylphosphine</a>; Dalton Transactions; Vol. 2004; No. 20; 3261-3272; <a href="https://doi.org/10.1039/B406692H">10.1039/B406692H</a></li>
<li>Yu, Steve S.-F. and Chen, Kelvin H.-C., el al. (2003) <a href="https://resolver.caltech.edu/CaltechAUTHORS:YUSjbact03">Production of High-Quality Particulate Methane Monooxygenase in High Yields from Methylococcus capsulatus (Bath) with a Hollow-Fiber Membrane Bioreactor</a>; Journal of Bacteriology; Vol. 185; No. 20; 5915-5924; PMCID PMC225036; <a href="https://doi.org/10.1128/JB.185.20.5915-5924.2003">10.1128/JB.185.20.5915-5924.2003</a></li>
<li>Chen, Pei-Yeh and Lin, Chun-Cheng, el al. (2002) <a href="https://resolver.caltech.edu/CaltechAUTHORS:CHEpnas02">One O-linked sugar can affect the coil-to-β structural transition of the prion peptide</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 99; No. 20; 12633-12638; PMCID PMC130512; <a href="https://doi.org/10.1073/pnas.192137799">10.1073/pnas.192137799</a></li>
<li>Zhong, Dongping and Pal, Sumir Kumar, el al. (2002) <a href="https://resolver.caltech.edu/CaltechAUTHORS:ZHOpnas02.1007">Femtosecond dynamics of rubredoxin: Tryptophan solvation and resonance energy transfer in the protein</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 99; No. 1; 13-18; PMCID PMC117505; <a href="https://doi.org/10.1073/pnas.012582399">10.1073/pnas.012582399</a></li>
<li>Schultz, Brian E. and Chan, Sunney I. (2001) <a href="https://resolver.caltech.edu/CaltechAUTHORS:SCHarbbs01">Structures and proton-pumping strategies of mitochondrial respiratory enzymes</a>; Annual Review of Biophysics and Biomolecular Structure; Vol. 30; 23-65; <a href="https://doi.org/10.1146/annurev.biophys.30.1.23">10.1146/annurev.biophys.30.1.23</a></li>
<li>Hansen, Kirk C. and Rock, Ronald S., el al. (2000) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170404-104411405">A Method for Photoinitating Protein Folding in a Nondenaturing Environment</a>; Journal of the American Chemical Society; Vol. 122; No. 46; 11567-11568; <a href="https://doi.org/10.1021/ja002949r">10.1021/ja002949r</a></li>
<li>Hung, Shao-Ching and Grant, Christopher V., el al. (2000) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20200219-114918387">ESEEM studies of succinate:ubiquinone reductase from Paracoccus denitrificans</a>; Journal of Biological Inorganic Chemistry; Vol. 5; No. 5; 593-602; <a href="https://doi.org/10.1007/s007750000142">10.1007/s007750000142</a></li>
<li>Hung, Shao-Ching and Grant, Christopher V., el al. (2000) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170419-092628378">Electron Spin−Lattice Relaxation Measurement of the 3Fe-4S (S-3) Cluster in Succinate:Ubiquinone Reductase from Paracoccus Denitrificans. A Detailed Analysis Based on a Dipole−Dipole Interaction Model</a>; Journal of Physical Chemistry A; Vol. 104; No. 19; 4402-4412; <a href="https://doi.org/10.1021/jp993693i">10.1021/jp993693i</a></li>
<li>Schultz, Brian E. and Hansen, Kirk C., el al. (2000) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170427-080241176">Rapid Photochemical Generation of Ubiquinol through a Radical Pathway: An Avenue for Probing Submillisecond Enzyme Kinetics</a>; Journal of Organic Chemistry; Vol. 65; No. 10; 3244-3247; <a href="https://doi.org/10.1021/jo000028t">10.1021/jo000028t</a></li>
<li>Cheng, Timothy C. and Ramakrishnan, Vijay, el al. (1999) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20120110-102835248">Purification and characterization of a cobalt-activated carboxypeptidase from the hyperthermophilic archaeon Pyrococcus furiosus</a>; Protein Science; Vol. 8; No. 11; 2474-2486; PMCID PMC2144183; <a href="https://doi.org/10.1110/ps.8.11.2474">10.1110/ps.8.11.2474</a></li>
<li>Schultz, Brian E. and Chan, Sunney I. (1998) <a href="https://resolver.caltech.edu/CaltechAUTHORS:SCHpnas98">Thermodynamics of electron transfer in Escherichia coli cytochrome bo(3)</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 95; No. 20; 11643-11648; PMCID PMC21694</li>
<li>Nguyen, Hiep-Hoa T. and Elliott, Sean J., el al. (1998) <a href="https://resolver.caltech.edu/CaltechAUTHORS:NGUjbc98">The Particulate Methane Monooxygenase from Methylococcus capsulatus (Bath) Is a Novel Copper-containing Three-subunit Enzyme: isolation and charactization</a>; Journal of Biological Chemistry; Vol. 273; No. 14; 7957-7966</li>
<li>Schultz, Brian E. and Edmondson, Dale E., el al. (1998) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170919-153418165">Reaction of Escherichia coli Cytochrome bo_3 with Substoichiometric Ubiquinol-2: A Freeze-Quench Electron Paramagnetic Resonance Investigation</a>; Biochemistry; Vol. 37; No. 12; 4160-4168; <a href="https://doi.org/10.1021/bi971714y">10.1021/bi971714y</a></li>
<li>Cavagnero, Silvia and Zhou, Zhi H., el al. (1998) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20171129-131714433">Unfolding Mechanism of Rubredoxin from Pyrococcus furiosus</a>; Biochemistry; Vol. 37; No. 10; 3377-3385; <a href="https://doi.org/10.1021/bi9721804">10.1021/bi9721804</a></li>
<li>Cavagnero, Silvia and Debe, Derek A., el al. (1998) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180524-152540450">Kinetic Role of Electrostatic Interactions in the Unfolding of Hyperthermophilic and Mesophilic Rubredoxins</a>; Biochemistry; Vol. 37; No. 10; 3369-3376; <a href="https://doi.org/10.1021/bi9721795">10.1021/bi9721795</a></li>
<li>Osborne, Jeffrey P. and Musser, Sigfried M., el al. (1998) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20200512-123507275">Rapid Formation of a Semiquinone Species on Oxidation of Quinol by the Cytochrome bo 3 Oxidase from Escherichia coli</a>; ISBN 978-4-431-68478-7; Oxygen Homeostasis and Its Dynamics; 33-39; <a href="https://doi.org/10.1007/978-4-431-68476-3_4">10.1007/978-4-431-68476-3_4</a></li>
<li>Waldeck, A. Reginald and Stowell, Michael H. B., el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20120125-131713605">Electron Paramagnetic Resonance Studies of Succinate:Ubiquinone Oxidoreductase from Paracoccus denitrificans</a>; Journal of Biological Chemistry; Vol. 272; No. 31; 19373-19382; <a href="https://doi.org/10.1074/jbc.272.31.19373">10.1074/jbc.272.31.19373</a></li>
<li>Schultz, Brian E. and Ye, Bao-Hui, el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180529-113543917">Electronic Paramagnetic Resonance and Magnetic Properties of Model Complexes for Binuclear Active Sites in Hydrolase Enzymes</a>; Inorganic Chemistry; Vol. 36; No. 12; 2617-2622; <a href="https://doi.org/10.1021/ic960988r">10.1021/ic960988r</a></li>
<li>Kwong, Daniel W. J. and Chan, O. Y., el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180529-114153019">DNA-Photocleavage Activities of Vanadium(V)−Peroxo Complexes</a>; Inorganic Chemistry; Vol. 36; No. 7; 1276-1277; <a href="https://doi.org/10.1021/ic960909b">10.1021/ic960909b</a></li>
<li>Bose, Salil and Hendler, Richard W., el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180213-085416151">Multichannel Analysis of Single-Turnover Kinetics of Cytochrome aa_3 Reduction of O_2</a>; Biochemistry; Vol. 36; No. 9; 2439-2449; <a href="https://doi.org/10.1021/bi9617419">10.1021/bi9617419</a></li>
<li>Musser, Siegfried M. and Stowell, Michael H. B., el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180212-130429431">Uncompetitive Substrate Inhibition and Noncompetitive Inhibition by 5-n-Undecyl-6-hydroxy-4,7-dioxobenzothiazole (UHDBT) and 2-n-Nonyl-4-hydroxyquinoline-N-oxide (NQNO) is Observed for the Cytochrome bo_3Complex: Implications for a Q(H_2)-Loop Proton Translocation Mechanism</a>; Biochemistry; Vol. 36; No. 4; 894-902; <a href="https://doi.org/10.1021/bi961723r">10.1021/bi961723r</a></li>
<li>Musser, Siegfried M. and Fann, Yang-Cheng, el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:MUSjbc97">Q-band electron nuclear double resonance (ENDOR) and X-band EPR of the sulfobetaine 12 heat-treated cytochrome c oxidase complex</a>; Journal of Biological Chemistry; Vol. 272; No. 1; 203-209</li>
<li>Stowell, Michael H. B. and Rock, Ronald S., el al. (1996) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150205-140522838">Efficient Synthesis of Photolabile Alkoxy Benzoin Protecting Groups</a>; Tetrahedron Letters; Vol. 37; No. 3; 307-310; <a href="https://doi.org/10.1016/0040-4039(95)02159-0">10.1016/0040-4039(95)02159-0</a></li>
<li>Evans, John Spencer and Chan, Sunney I., el al. (1995) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20190227-091746936">Prediction of polyelectrolyte polypeptide structures using Monte Carlo conformational search methods with implicit solvation modeling</a>; Protein Science; Vol. 4; No. 10; 2019-2031; PMCID PMC2142998; <a href="https://doi.org/10.1002/pro.5560041007">10.1002/pro.5560041007</a></li>
<li>DiMagno, Theodore J. and Stowell, Michael H. B., el al. (1995) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180525-111314381">Nitrobenzene &quot;Caged&quot; Compounds as Irreversible Photoreductants: A Rational Approach to Studying Photoinduced Intermolecular Electron-Transfer Reactions in Proteins</a>; Journal of Physical Chemistry; Vol. 99; No. 34; 13038-13047; <a href="https://doi.org/10.1021/j100034a052">10.1021/j100034a052</a></li>
<li>Cavagnero, Silvia and Zhou, Zhi H., el al. (1995) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20171120-141844682">Response of Rubredoxin from Pyrococcus furiosus to Environmental Changes: Implications for the Origin of Hyperthermostability</a>; Biochemistry; Vol. 34; No. 31; 9865-9873; <a href="https://doi.org/10.1021/bi00031a007">10.1021/bi00031a007</a></li>
<li>Evans, John Spencer and Mathiowetz, Alan M., el al. (1995) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20190301-092706779">De novo prediction of polypeptide conformations using dihedral probability grid Monte Carlo methodology</a>; Protein Science; Vol. 4; No. 6; 1203-1216; PMCID PMC2143148; <a href="https://doi.org/10.1002/pro.5560040618">10.1002/pro.5560040618</a></li>
<li>Lin, Jian and Wu, Shuguang, el al. (1995) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180205-074945747">Electron Transfer from Cytochrome c to 8-azido-ATP-Modified Cytochrome c Oxidase</a>; Biochemistry; Vol. 34; No. 19; 6335-6343; <a href="https://doi.org/10.1021/bi00019a011">10.1021/bi00019a011</a></li>
<li>Lin, Jian and Wu, Shuguang, el al. (1995) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180205-083519723">8-Azido-ATP Modification of Cytochrome c: Retardation of Its Electron-Transfer Activity to Cytochrome c Oxidase</a>; Biochemistry; Vol. 34; No. 8; 2678-2685; <a href="https://doi.org/10.1021/bi00008a035">10.1021/bi00008a035</a></li>
<li>Stowell, Michael H. B. and Larsen, Randy W., el al. (1993) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150205-142230754">Transient electron-transfer studies on the two-subunit cytochrome c oxidase from Paracoccus denitrificans</a>; Journal of Physical Chemistry; Vol. 97; No. 12; 3054-3057; <a href="https://doi.org/10.1021/j100114a036">10.1021/j100114a036</a></li>
<li>Lou, Bih Show and Larsen, Randy W., el al. (1993) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170408-155639902">Conformational dependence of carbon monoxide ligation dynamics in cytochrome c oxidase</a>; Journal of the American Chemical Society; Vol. 115; No. 2; 403-407; <a href="https://doi.org/10.1021/ja00055a006">10.1021/ja00055a006</a></li>
<li>Wang, Jianling and Larsen, Randy W., el al. (1992) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180724-152024973">Ligand photodissociation and recombination dynamics of ferrous cytochrome c peroxidase at alkaline pH</a>; Journal of the American Chemical Society; Vol. 114; No. 4; 1487-1488; <a href="https://doi.org/10.1021/ja00030a057">10.1021/ja00030a057</a></li>
<li>Larsen, Randy W. and Pan, Lian-Ping, el al. (1992) <a href="https://resolver.caltech.edu/CaltechAUTHORS:LARpnas92">Could CuB be the site of redox linkage in cytochrome c oxidase?</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 89; No. 2; 723-727; PMCID PMC48311</li>
<li>Larsen, Randy W. and Li, Wei, el al. (1990) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180212-143012991">Room temperature characterization of the dioxygen intermediates of cytochrome c oxidase by resonance Raman spectroscopy</a>; Biochemistry; Vol. 29; No. 43; 10135-10140; <a href="https://doi.org/10.1021/bi00495a018">10.1021/bi00495a018</a></li>
<li>Watnick, Paula I. and Chan, Sunney I., el al. (1990) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20180212-141345237">Hydrophobic mismatch in gramicidin A'/Lecithin systems</a>; Biochemistry; Vol. 29; No. 26; 6215-6221; <a href="https://doi.org/10.1021/bi00478a015">10.1021/bi00478a015</a></li>
<li>Watnick, Paula I. and Dea, Phoebe, el al. (1990) <a href="https://resolver.caltech.edu/CaltechAUTHORS:WATpnas90">Characterization of the transverse relaxation rates in lipid bilayers</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 87; No. 6; 2082-2086; PMCID PMC53630</li>
<li>Chan, Sunney I. and Li, Peter Mark (1990) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20171107-152051230">Cytochrome c oxidase: understanding nature's design of a proton pump</a>; Biochemistry; Vol. 29; No. 1; 1-12; <a href="https://doi.org/10.1021/bi00453a001">10.1021/bi00453a001</a></li>
<li>Copeland, Robert A. and Chan, Sunney I. (1989) <a href="https://resolver.caltech.edu/CaltechAUTHORS:COParpc89">Proton translocation in proteins</a>; Annual Review of Physical Chemistry; Vol. 40; 671-698; <a href="https://doi.org/10.1146/annurev.pc.40.100189.003323">10.1146/annurev.pc.40.100189.003323</a></li>
<li>Wang, Jin-Feng and Falke, Joseph J., el al. (1986) <a href="https://resolver.caltech.edu/CaltechAUTHORS:WANpnas86">A proton NMR study of the mechanism of the erythrocyte glucose transporter</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 10; 3277-3281; PMCID PMC323496</li>
<li>Falke, Joseph J. and Kanes, Katherine J., el al. (1985) <a href="https://resolver.caltech.edu/CaltechAUTHORS:FALjbc85c">The minimal structure containing the band 3 anion transport site. A 35Cl NMR study</a>; Journal of Biological Chemistry; Vol. 260; No. 24; 13294-13303</li>
<li>Falke, Joseph J. and Chan, Sunney I. (1985) <a href="https://resolver.caltech.edu/CaltechAUTHORS:FALjbc85b">Evidence that anion transport by band 3 proceeds via a ping-pong mechanism involving a single transport site. A 35 Cl NMR study</a>; Journal of Biological Chemistry; Vol. 260; No. 17; 9537-9544</li>
<li>Falke, Joseph J. and Kanes, Katherine J., el al. (1985) <a href="https://resolver.caltech.edu/CaltechAUTHORS:FALjbc85a">The kinetic equation for the chloride transport cycle of band 3. A 35Cl and 37Cl NMR study</a>; Journal of Biological Chemistry; Vol. 260; No. 17; 9545-9551</li>
<li>Martin, Craig T. and Scholes, Charles P., el al. (1985) <a href="https://resolver.caltech.edu/CaltechAUTHORS:MARjbc85">The identification of histidine ligands to cytochrome a in cytochrome c oxidase</a>; Journal of Biological Chemistry; Vol. 260; No. 5; 2857-2861</li>
<li>Brudvig, Gary W. and Blair, David F., el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20120629-110323859">Electron Spin Relaxation of Cu_A and Cytochrome a in Cytochrome c Oxidase. Comparison to heme, copper, and sulfur radical complexes</a>; Journal of Biological Chemistry; Vol. 259; No. 17; 11001-11009</li>
<li>Falke, Joseph J. and Pace, R. J., el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:FALjbc84b">Chloride binding to the anion transport binding sites of band 3. A 35Cl NMR study</a>; Journal of Biological Chemistry; Vol. 259; No. 10; 6472-6480</li>
<li>Falke, Joseph J. and Chan, Sunney I., el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:FALjbc84a">Halide binding by the purified halorhodopsin chromoprotein. II. New chloride-binding sites revealed by 35Cl NMR</a>; Journal of Biological Chemistry; Vol. 259; No. 4; 2185-2189</li>
<li>Stevens, Tom H. and Martin, Craig T., el al. (1982) <a href="https://resolver.caltech.edu/CaltechAUTHORS:STEjbc82">The nature of CuA in cytochrome c oxidase</a>; Journal of Biological Chemistry; Vol. 257; No. 20; 12106-10113</li>
<li>Stevens, Tom H. and Chan, Sunney I. (1981) <a href="https://resolver.caltech.edu/CaltechAUTHORS:STEjbc81">Histidine is the axial ligand to cytochrome alpha 3 in cytochrome c oxidase</a>; Journal of Biological Chemistry; Vol. 256; No. 3; 1069-1071</li>
<li>Bocian, David F. and Lemley, Ann T., el al. (1979) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20160815-122514293">Resonance Raman Spectra of Cytochrome c Oxidase. Excitation in the 600-nm Region</a>; Biochemistry; Vol. 18; No. 20; 4396-4402; <a href="https://doi.org/10.1021/bi00587a020">10.1021/bi00587a020</a></li>
<li>Stevens, Tom H. and Brudvig, Gary W., el al. (1979) <a href="https://resolver.caltech.edu/CaltechAUTHORS:STEpnas79">Structure of cytochrome a3-Cua3 couple in cytochrome c oxidase as revealed by nitric oxide binding studies</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 76; No. 7; 3320-3324; PMCID PMC383817</li>
<li>Bocian, David F. and Chan, Sunney I. (1978) <a href="https://resolver.caltech.edu/CaltechAUTHORS:BOCarpc78">NMR studies of membrane structure and dynamics</a>; Annual Review of Physical Chemistry; Vol. 29; 307-335; <a href="https://doi.org/10.1146/annurev.pc.29.100178.001515">10.1146/annurev.pc.29.100178.001515</a></li>
<li>Hu, Valerie W. and Chan, Sunney I., el al. (1977) <a href="https://resolver.caltech.edu/CaltechAUTHORS:HUVpnas77">X-ray absorption edge studies on oxidized and reduced cytochrome c oxidase</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 74; No. 9; 3821-3825; PMCID PMC431745</li>
<li>Lau, Arthur L. Y. and Chan, Sunney I. (1975) <a href="https://resolver.caltech.edu/CaltechAUTHORS:LAUpnas75">Alamethicin-mediated fusion of lecithin vesicles</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 72; No. 6; 2170-2174; PMCID PMC432718</li>
<li>Dea, Phoebe and Chan, Sunney I., el al. (1972) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150728-154738893">High-Resolution Proton Magnetic Resonance Spectra of a Rabbit Sciatic Nerve</a>; Science; Vol. 175; No. 4018; 206-209; <a href="https://doi.org/10.1126/science.175.4018.206">10.1126/science.175.4018.206</a></li>
<li>Chan, Sunney I. and Lin, L., el al. (1970) <a href="https://resolver.caltech.edu/CaltechAUTHORS:CHApnas70">The anomalous deuterium isotope effect on the chemical shift of the bridge hydrogen in the enol tautomer of 2,4-pentanedione</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 65; No. 4; 816-822; PMCID PMC282988</li>
<li>Glaser, Michael and Simpkins, Henry, el al. (1970) <a href="https://resolver.caltech.edu/CaltechAUTHORS:GLApnas70">On the interactions of lipids and proteins in the red blood cell membrane</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 65; No. 3; 721-728; PMCID PMC282966</li>
<li>Manatt, Stanley and Elleman, Daniel D., el al. (1970) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150211-111941293">Magnetic Resonance Studies of Lunar Samples</a>; Science; Vol. 167; No. 3918; 709-711; <a href="https://doi.org/10.1126/science.167.3918.709">10.1126/science.167.3918.709</a></li>
<li>Raftery, M. A. and Dahlquist, F. W., el al. (1968) <a href="https://resolver.caltech.edu/CaltechAUTHORS:RAFjbc68">A Proton Magnetic Resonance Study of the Association of Lysozyme with Monosaccharide Inhibitors</a>; Journal of Biological Chemistry; Vol. 243; No. 16; 4175-4180</li>
<li>Bangerter, Benedict W. and Chan, Sunney I. (1968) <a href="https://resolver.caltech.edu/CaltechAUTHORS:BANpnas68">A Proton Magnetic Resonance Study of The Interaction of Adenosine with Polyuridylic Acid: Evidence for Both Adenine-Uracil Base-Stacking and Base-Pairing</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 60; No. 4; 1144-1151; PMCID PMC224893</li>
<li>Chan, Sunney I. and Bangerter, Benedict W., el al. (1966) <a href="https://resolver.caltech.edu/CaltechAUTHORS:CHApnas66">Purine binding to dinucleotides: Evidence for base stacking and insertion</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 55; No. 4; 720-727; PMCID PMC224219</li>
</ul>