<h1>Richards, John H.</h1>
<h2>Article from <a href="https://authors.library.caltech.edu">CaltechAUTHORS</a></h2>
<ul>
<li>Warren, Jeffrey J. and Lancaster, Kyle M., el al. (2012) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20121126-112150310">Inner- and outer-sphere metal coordination in blue copper proteins</a>; Journal of Inorganic Biochemistry; Vol. 115; 119-126; PMCID PMC3434318; <a href="https://doi.org/10.1016/j.jinorgbio.2012.05.002">10.1016/j.jinorgbio.2012.05.002</a></li>
<li>Lancaster, Kyle M. and Zaballa, María-Eugenia, el al. (2012) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20120611-154824690">Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins</a>; Journal of the American Chemical Society; Vol. 134; No. 19; 8241-8253; PMCID PMC4794991; <a href="https://doi.org/10.1021/ja302190r">10.1021/ja302190r</a></li>
<li>Potapov, Alexey and Lancaster, Kyle M., el al. (2012) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20120515-154220333">Spin Delocalization Over Type Zero Copper</a>; Inorganic Chemistry; Vol. 51; No. 7; 4066-4075; PMCID PMC3322426; <a href="https://doi.org/10.1021/ic202336m">10.1021/ic202336m</a></li>
<li>Lancaster, Kyle M. and Farver, Ole, el al. (2011) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20110429-103650204">Electron Transfer Reactivity of Type Zero Pseudomonas aeruginosa Azurin</a>; Journal of the American Chemical Society; Vol. 133; No. 13; 4865-4873; PMCID PMC3607328; <a href="https://doi.org/10.1021/ja1093919">10.1021/ja1093919</a></li>
<li>Lancaster, Kyle M. and Sproules, Stephen, el al. (2010) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20101027-093220417">Outer-Sphere Effects on Reduction Potentials of Copper Sites in Proteins: The Curious Case of High Potential Type 2 C112D/M121E Pseudomonas aeruginosa Azurin</a>; Journal of the American Chemical Society; Vol. 132; No. 41; 14590-14595; PMCID PMC3375907; <a href="https://doi.org/10.1021/ja105731x">10.1021/ja105731x</a></li>
<li>Lancaster, Kyle M. and George, Serena DeBeer, el al. (2009) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20100107-092654651">Type-zero copper proteins</a>; Nature Chemistry; Vol. 1; No. 9; 711-715; PMCID PMC2841405; <a href="https://doi.org/10.1038/NCHEM.412">10.1038/NCHEM.412</a></li>
<li>Lancaster, Kyle M. and Yokoyama, Keiko, el al. (2009) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20090910-101427356">High-Potential C112D/M121X (X = M, E, H, L) Pseudomonas aeruginosa Azurins</a>; Inorganic Chemistry; Vol. 48; No. 4; 1278-1280; PMCID PMC2765487; <a href="https://doi.org/10.1021/ic802322e">10.1021/ic802322e</a></li>
<li>Shih, Crystal and Museth, Anna Katrine, el al. (2008) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20141118-091949973">Tryptophan-Accelerated Electron Flow Through Proteins</a>; Science; Vol. 320; No. 5884; 1760-1762; <a href="https://doi.org/10.1126/science.1158241">10.1126/science.1158241</a></li>
<li>Yokoyama, Keiko and Leigh, Brian S., el al. (2008) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150424-150000195">Electron Tunneling through Pseudomonas aeruginosa Azurins on SAM Gold Electrodes</a>; Inorganica Chimica Acta; Vol. 361; No. 4; 1095-1099; PMCID PMC2390814; <a href="https://doi.org/10.1016/j.ica.2007.08.022">10.1016/j.ica.2007.08.022</a></li>
<li>Kim, Judy E. and Arjara, Gitrada, el al. (2006) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150424-152416156">Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence</a>; Journal of Physical Chemistry B; Vol. 110; No. 35; 17656-62; PMCID PMC2519049; <a href="https://doi.org/10.1021/jp061991r">10.1021/jp061991r</a></li>
<li>Blanco-Rodríguez, Ana María and Busby, Michael, el al. (2006) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20170405-145213550">Excited-State Dynamics of Structurally Characterized [Re^I(CO)_3(phen)(HisX)]^+(X = 83, 109) Pseudomonas aeruginosa Azurins in Aqueous Solution</a>; Journal of the American Chemical Society; Vol. 128; No. 13; 4365-4370; <a href="https://doi.org/10.1021/ja057451+">10.1021/ja057451+</a></li>
<li>Blanco-Rodríguez, Ana María and Busby, Michael, el al. (2006) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150424-145943126">Excited-State Dynamics of Structurally Characterized [Re^I(CO)_3(phen)(HisX)]^+ (X = 83, 109) Pseudomonas aeruginosa Azurins in Aqueous Solution</a>; Journal of the American Chemical Society; Vol. 128; No. 13; 4365-4370; <a href="https://doi.org/10.1021/ja057451+">10.1021/ja057451+</a></li>
<li>Fujita, Kyoko and Nakamura, Nobufumi, el al. (2004) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150424-154505770">Mimicking protein-protein electron transfer: voltammetry of Pseudomonas aeruginosa azurin and the Thermus thermophilus Cu_A domain at ω-derivatized self-assembled-monolayer gold electrodes</a>; Journal of the American Chemical Society; Vol. 126; No. 43; 13954-61; <a href="https://doi.org/10.1021/ja047875o">10.1021/ja047875o</a></li>
<li>Niki, Katsumi and Hardy, W. Reef, el al. (2003) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-140736351">Coupling to Lysine-13 Promotes Electron Tunneling through Carboxylate-Terminated Alkanethiol Self-Assembled Monolayers to Cytochrome c</a>; Journal of Physical Chemistry B; Vol. 107; No. 37; 9947-9949; <a href="https://doi.org/10.1021/jp035392l">10.1021/jp035392l</a></li>
<li>McGuirl, Michele A. and Lee, Jennifer C., el al. (2003) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150424-155358251">Cloning, heterologous expression, and characterization of recombinant class II cytochromes c from Rhodopseudomonas palustris</a>; Biochimica et Biophysica Acta - General Subjects; Vol. 1619; No. 1; 23-8; <a href="https://doi.org/10.1016/S0304-4165(02)00437-3">10.1016/S0304-4165(02)00437-3</a></li>
<li>Machczynski, Michael C. and Gray, Harry B., el al. (2002) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150424-155358996">An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins</a>; Journal of Inorganic Biochemistry; Vol. 88; No. 3-4; 375-80; <a href="https://doi.org/10.1016/S0162-0134(02)00364-1">10.1016/S0162-0134(02)00364-1</a></li>
<li>Fernández, Claudio O. and Cricco, Julia A., el al. (2001) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-115753848">Axial Ligand Modulation of the Electronic Structures of Binuclear Copper Sites:  Analysis of Paramagnetic ^1H NMR Spectra of Met160Gln Cu_A</a>; Journal of the American Chemical Society; Vol. 123; No. 47; 11678-11685; <a href="https://doi.org/10.1021/ja0162515">10.1021/ja0162515</a></li>
<li>Slutter, Claire E. and Gromov, Igor, el al. (2001) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-150114010">Pulsed EPR/ENDOR Characterization of Perturbations of the Cu_A Center Ground State by Axial Methionine Ligand Mutations</a>; Journal of the American Chemical Society; Vol. 123; No. 22; 5325-5336; <a href="https://doi.org/10.1021/ja003924v">10.1021/ja003924v</a></li>
<li>Di Bilio, Angel J. and Crane, Brian R., el al. (2001) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-143033571">Properties of Photogenerated Tryptophan and Tyrosyl Radicals in Structurally Characterized Proteins Containing Rhenium(I) Tricarbonyl Diimines</a>; Journal of the American Chemical Society; Vol. 123; No. 13; 3181-3182; <a href="https://doi.org/10.1021/ja0043183">10.1021/ja0043183</a></li>
<li>Webb, M. Adam and Kiser, Cynthia N., el al. (2000) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-154244398">Resonance Raman Spectroscopy of Met121Glu Azurin</a>; Journal of Physical Chemistry B; Vol. 104; No. 46; 10915-10920; <a href="https://doi.org/10.1021/jp000832j">10.1021/jp000832j</a></li>
<li>Winkler, Jay R. and Di Bilio, Angel J., el al. (1999) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-092352002">Electron tunneling in biological molecules</a>; Pure and Applied Chemistry; Vol. 71; No. 9; 1753-1764; <a href="https://doi.org/10.1351/pac199971091753">10.1351/pac199971091753</a></li>
<li>Slutter, Claire E. and Gromov, Igor, el al. (1999) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-161643812">Mutations of the Weak Axial Ligand in the Thermus CuA Center Modulates Its Electronic Structure</a>; Journal of the American Chemical Society; Vol. 121; No. 21; 5077-5078; <a href="https://doi.org/10.1021/ja984361e">10.1021/ja984361e</a></li>
<li>DeBeer, Serena and Kiser, Cynthia N., el al. (1999) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150424-155359723">X-ray Absorption Spectra of the Oxidized and Reduced Forms of C112D Azurin from Pseudomonas aeruginosa</a>; Inorganic Chemistry; Vol. 38; No. 3; 433-438; <a href="https://doi.org/10.1021/ic9804622">10.1021/ic9804622</a></li>
<li>Regan, J. J. and Di Bilio, A. J., el al. (1998) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150427-151804934">Electron tunneling in Ru-modified His46Asp azurin. Coupling through the Cu ligands</a>; Inorganica Chimica Acta; Vol. 275-276; No. 1-2; 470-480; <a href="https://doi.org/10.1016/S0020-1693(98)00066-8">10.1016/S0020-1693(98)00066-8</a></li>
<li>Vila, A. J. and Ramirez, B. E., el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-132741371">Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas aeruginosa His46Asp Azurin</a>; Inorganic Chemistry; Vol. 36; No. 20; 4567-4570; <a href="https://doi.org/10.1021/ic9703282">10.1021/ic9703282</a></li>
<li>Faham, Salem and Mizoguchi, Tadashi J., el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150205-135731010">Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the Cu^(II(Cys112Asp) protein</a>; Journal of Biological Inorganic Chemistry; Vol. 2; No. 4; 464-469; <a href="https://doi.org/10.1007/s007750050157">10.1007/s007750050157</a></li>
<li>Vanhove, Marc and Guillaume, Gilliane, el al. (1997) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150427-161237094">Kinetic and thermodynamic consequences of the removal of the Cys-77–Cys-123 disulphide bond for the folding of TEM-1 β-lactamase</a>; Biochemical Journal; Vol. 321; No. Part 2; 413-417</li>
<li>Immoos, Chad and Hill, Michael G., el al. (1996) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150427-150735788">Electrochemistry of the Cu_A domain of Thermus thermophilus cytochrome ba _3</a>; Journal of Biological Inorganic Chemistry; Vol. 1; No. 6; 529-531; <a href="https://doi.org/10.1007/s007750050088">10.1007/s007750050088</a></li>
<li>Bertini, Ivano and Bren, Kara L., el al. (1996) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-120953603">The Cu_A Center of a Soluble Domain from Thermus Cytochrome ba_3. An NMR Investigation of the Paramagnetic Protein</a>; Journal of the American Chemical Society; Vol. 118; No. 46; 11658-11659; <a href="https://doi.org/10.1021/ja9621410">10.1021/ja9621410</a></li>
<li>McCleskey, T. Mark and Mizoguchi, Tadashi J., el al. (1996) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150424-155400474">Electronic Spectroscopy of Gold(I) Pseudomonasaeruginosa Azurin Derivatives</a>; Inorganic Chemistry; Vol. 35; No. 11; 3434-3435; <a href="https://doi.org/10.1021/ic951055i">10.1021/ic951055i</a></li>
<li>Slutter, Claire E. and Sanders, Donita, el al. (1996) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-122517025">Water-Soluble, Recombinant Cu_A-Domain of the Cytochrome ba_3 Subunit II from Thermus thermophilus</a>; Biochemistry; Vol. 35; No. 11; 3387-3395; <a href="https://doi.org/10.1021/bi9525839">10.1021/bi9525839</a></li>
<li>Slutter, Claire E. and Langen, Ralf, el al. (1996) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-074946222">Electron-transfer studies with the CuA domain of Thermus thermophilus cytochrome ba_3</a>; Inorganica Chimica Acta; Vol. 243; No. 1-2; 141-145; <a href="https://doi.org/10.1016/0020-1693(95)04901-0">10.1016/0020-1693(95)04901-0</a></li>
<li>Hay, Michael and Richards, John H., el al. (1996) <a href="https://resolver.caltech.edu/CaltechAUTHORS:HAYpnas96">Construction and characterization of an azurin analog for the purple copper site in cytochrome c oxidase</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 93; No. 1; 461-464; PMCID PMC40258; <a href="https://doi.org/10.1073/pnas.93.1.461">10.1073/pnas.93.1.461</a></li>
<li>Langen, Ralf and Chang, I-Jy, el al. (1995) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150116-145929070">Electron Tunneling in Proteins: Coupling Through a β Strand</a>; Science; Vol. 268; No. 5218; 1733-1735; <a href="https://doi.org/10.1126/science.7792598">10.1126/science.7792598</a></li>
<li>Piccioli, Mario and Luchinat, Claudio, el al. (1995) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-131303284">Paramagnetic NMR spectroscopy and coordination structure of cobalt(II) Cys112Asp azurin</a>; Inorganic Chemistry; Vol. 34; No. 3; 737-742; <a href="https://doi.org/10.1021/ic00107a027">10.1021/ic00107a027</a></li>
<li>Casimiro, Danilo R. and Richards, John H., el al. (1993) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150430-135530174">Electron Transfer in Ruthenium-Modified Cytochromes c. σ-Tunneling Pathways through Aromatic Residues</a>; Journal of Physical Chemistry; Vol. 97; No. 50; 13073-13077; <a href="https://doi.org/10.1021/j100152a007">10.1021/j100152a007</a></li>
<li>Lu, Yi and Casimiro, Danilo R., el al. (1993) <a href="https://resolver.caltech.edu/CaltechAUTHORS:LUYpnas93">Structurally engineered cytochromes with unusual ligand-binding properties: Expression of Saccharomyces cerevisiae Met-80 --&gt; Ala iso-1-cytochrome c</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 90; No. 24; 11456-11459; PMCID PMC48002</li>
<li>Germanas, Juris P. and Di Bilio, Angel J., el al. (1993) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150430-160127576">Site saturation of the histidine-46 position in Pseudomonas aeruginosa azurin: Characterization of the His46Asp copper and cobalt proteins</a>; Biochemistry; Vol. 32; No. 30; 7698-7702; <a href="https://doi.org/10.1021/bi00081a014">10.1021/bi00081a014</a></li>
<li>Casimiro, Danilo R. and Wong, Luet-L., el al. (1993) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150430-135323908">Electron Transfer in Ruthenium/Zinc Porphyrin Derivatives of
Recombinant Human Myoglobins. Analysis of Tunneling Pathways in Myoglobin and Cytochrome c</a>; Journal of the American Chemical Society; Vol. 115; No. 4; 1485-1489; <a href="https://doi.org/10.1021/ja00057a037">10.1021/ja00057a037</a></li>
<li>Mizoguchi, Tadashi J. and Di Bilio, Angel J., el al. (1992) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-113949666">Blue to type 2 binding. Copper(II) and cobalt(II) derivatives of a Cys112Asp mutant of Pseudomonas aeruginosa azurin</a>; Journal of the American Chemical Society; Vol. 114; No. 25; 10076-10078; <a href="https://doi.org/10.1021/ja00051a059">10.1021/ja00051a059</a></li>
<li>Smith, Eugene T. and Tomich, John M., el al. (1991) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150501-115533799">A totally synthetic histidine-2 ferredoxin: thermal stability and redox properties</a>; Biochemistry; Vol. 30; No. 50; 11669-11676; <a href="https://doi.org/10.1021/bi00114a009">10.1021/bi00114a009</a></li>
<li>Chang, Thomas K. and Iverson, Sheila A., el al. (1991) <a href="https://resolver.caltech.edu/CaltechAUTHORS:CHApnas91">Gene Synthesis, Expression, and Mutagenesis of the Blue Copper Proteins Azurin and Plastocyanin</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 88; No. 4; 1325-1329; PMCID PMC51010; <a href="https://doi.org/10.1073/pnas.88.4.1325">10.1073/pnas.88.4.1325</a></li>
<li>Smith, Eugene T. and Feinberg, Benjamin A., el al. (1991) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-123928699">Physical characterization of a totally synthetic 2[4Fe-4S] clostridial ferredoxin</a>; Journal of the American Chemical Society; Vol. 113; No. 2; 688-689; <a href="https://doi.org/10.1021/ja00002a055">10.1021/ja00002a055</a></li>
<li>Chang, Yie-Hwa and Labgold, Marc R., el al. (1990) <a href="https://resolver.caltech.edu/CaltechAUTHORS:CHApnas90b">Altering Enzymatic Activity: Recruitment of Carboxypeptidase Activity into an RTEM β-Lactamase/Penicillin-Binding Protein 5 Chimera</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 87; No. 7; 2823-2827; PMCID PMC53783; <a href="https://doi.org/10.1073/pnas.87.7.2823">10.1073/pnas.87.7.2823</a></li>
<li>Bowler, Bruce E. and Meade, Thomas J., el al. (1989) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20110620-160433811">Long-range electron transfer in structurally engineered pentaammineruthenium (histidine-62) cytochrome c</a>; Journal of the American Chemical Society; Vol. 111; No. 23; 8757-8759; <a href="https://doi.org/10.1021/ja00205a049">10.1021/ja00205a049</a></li>
<li>Healey, William J. and Labgold, Marc R., el al. (1989) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150430-075008534">Substrate specificities in class A β-lactamases: Preference for penams vs. cephams. The role of residues 237</a>; Proteins; Vol. 6; No. 3; 275-283; <a href="https://doi.org/10.1002/prot.340060310">10.1002/prot.340060310</a></li>
<li>Tomich, John M. and Carson, L. Wulf, el al. (1988) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-074254869">Prevention of Aggregation of Synthetic Membrane-Spanning Peptides by Addition of Detergent</a>; Analytical Biochemistry; Vol. 174; No. 1; 197-203; <a href="https://doi.org/10.1016/0003-2697(88)90535-0">10.1016/0003-2697(88)90535-0</a></li>
<li>Roise, David and Theiler, Franziska, el al. (1988) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-125902591">Amphiphilicity is essential for mitochondrial presequence function</a>; EMBO Journal; Vol. 7; No. 3; 649-653; PMCID PMC454369; <a href="https://doi.org/10.1002/j.1460-2075.1988.tb02859.x">10.1002/j.1460-2075.1988.tb02859.x</a></li>
<li>Foster, Patricia L. and Dalbadie-McFarland, Gloria, el al. (1987) <a href="https://resolver.caltech.edu/CaltechAUTHORS:FOSjbact87">Creation of a test plasmid for detecting G-C-to-T-A transversions by changing serine to arginine in the active site of beta-lactamase</a>; Journal of Bacteriology; Vol. 169; No. 6; 2476-2481; PMCID PMC212096</li>
<li>Schultz, Steve C. and Dalbadie-McFarland, Gloria, el al. (1987) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-092022777">Stability of wild-type and mutant RTEM-1 β-lactamases: Effect of the disulfide bond</a>; Proteins; Vol. 2; No. 4; 290-297; <a href="https://doi.org/10.1002/prot.340020405">10.1002/prot.340020405</a></li>
<li>Carroll, Steven S. and Richards, John H. (1987) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-160116595">Progress Toward the Rational Study of Enzyme Structure-Function Relationships</a>; Annual Reports in Medicinal Chemistry; Vol. 22; 293-301</li>
<li>Schultz, Steve C. and Richards, John H. (1986) <a href="https://resolver.caltech.edu/CaltechAUTHORS:SCHUpnas86">Site-saturation studies of β-lactamase: Production and characterization of mutant β-lactamases with all possible amino acid substitutions at residue 71</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 6; 1588-1592; PMCID PMC323128; <a href="https://doi.org/10.1073/pnas.83.6.1588">10.1073/pnas.83.6.1588</a></li>
<li>Dalbadie-McFarland, Gloria and Neitzel, James J., el al. (1986) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-142317225">Active-site mutants of β-lactamase: use of an inactive double mutant to study requirements for catalysis</a>; Biochemistry; Vol. 25; No. 2; 332-338; <a href="https://doi.org/10.1021/bi00350a008">10.1021/bi00350a008</a></li>
<li>Roise, David and Horvath, Suzanna J., el al. (1986) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-161442866">A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers</a>; EMBO Journal; Vol. 5; No. 6; 1327-1334; PMCID PMC1166944</li>
<li>Lad, P. M. and Glovsky, M. M., el al. (1985) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-084710345">Regulation of human neutrophil guanylate cyclase by metal ions, free radicals and the muscarinic cholinergic receptor</a>; Molecular Immunology; Vol. 22; No. 7; 731-739; <a href="https://doi.org/10.1016/0161-5890(85)90138-5">10.1016/0161-5890(85)90138-5</a></li>
<li>Dalbadie-McFarland, G. and Neitzel, J., el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-154055761">Studies of Protein Function by Various Mutagenic Strategies: β-Lactamase</a>; Annals of the New York Academy of Sciences; Vol. 434; 232-238; <a href="https://doi.org/10.1111/j.1749-6632.1984.tb29833.x">10.1111/j.1749-6632.1984.tb29833.x</a></li>
<li>Lad, P. M. and Glovsky, M. M., el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-075621107">Identification of receptor regulatory proteins, membrane glycoproteins, and functional characteristics of adenylate cyclase in vesicles derived from the human neutrophil</a>; Molecular Immunology; Vol. 21; No. 7; 627-639; <a href="https://doi.org/10.1016/0161-5890(84)90048-8">10.1016/0161-5890(84)90048-8</a></li>
<li>Dalbadie-McFarland, G. and Riggs, A. D., el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150430-084326616">Directed mutagenesis as a technique to study protein function: application to β-lactamase</a>; Biochemical Society Transactions; Vol. 12; No. 2; 226-228; <a href="https://doi.org/10.1042/bst0120226">10.1042/bst0120226</a></li>
<li>Lad, Pramod M. and Glovsky, M. Michael, el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-130345352">The β-adrenergic receptor in the human neutrophil plasma membrane: receptor-cyclase uncoupling is associated with amplified GTP activation</a>; Journal of Immunology; Vol. 132; No. 3; 1466-1471</li>
<li>Goers, John W. and Glovsky, M. Michael, el al. (1984) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-115820659">Studies on C3a_(hu) Binding to Human Eosinophils: Characterization of Binding</a>; International Archives of Allergy and Applied Immunology; Vol. 74; No. 2; 147-151; <a href="https://doi.org/10.1159/000233535">10.1159/000233535</a></li>
<li>Perkins, T. and Satterlee, J. D., el al. (1983) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-075633642">Mechanism of T_1 relaxation in ^(13)CO complexed to an iron porphyrin: implications for CO bonding in heme proteins</a>; Journal of the American Chemical Society; Vol. 105; No. 5; 1350-1354; <a href="https://doi.org/10.1021/ja00343a047">10.1021/ja00343a047</a></li>
<li>Dalbadie-McFarland, G. and Cohen, L. W., el al. (1982) <a href="https://resolver.caltech.edu/CaltechAUTHORS:DALpnas82">Oligonucleotide-Directed Mutagenesis as a General and Powerful Method for Studies of Protein Function</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 79; No. 21; 6409-6413</li>
<li>McGee, Dennis E. and Carroll, Steven S., el al. (1982) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-072043087">Diol dehydratase: N-terminal amino acid sequences and subunit stoichiometry</a>; Biochemical and Biophysical Research Communications; Vol. 108; No. 2; 547-551; <a href="https://doi.org/10.1016/0006-291X(82)90863-4">10.1016/0006-291X(82)90863-4</a></li>
<li>Richards, J. H. and Teeri, J. A. (1982) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150430-135659316">Re-evaluation of proposed C_4 photosynthetic characteristics in the genus Larix</a>; Physiologia Plantarum; Vol. 55; No. 2; 117-120; <a href="https://doi.org/10.1111/j.1399-3054.1982.tb02273.x">10.1111/j.1399-3054.1982.tb02273.x</a></li>
<li>Bachovchin, William W. and Kaiser, Robert, el al. (1981) <a href="https://resolver.caltech.edu/CaltechAUTHORS:BACpnas81">Catalytic Mechanism of Serine Proteases: Reexamination of the pH Dependence of the Histidyl 1J{13C2-H} Coupling Constant in the Catalytic Triad of alpha-lytic Protease</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 78; No. 12; 7323-7326</li>
<li>McGee, Dennis E. and Richards, John H. (1981) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150427-144355211">Purification and subunit characterization of propanediol dehydratase, a membrane-associated enzyme</a>; Biochemistry; Vol. 20; No. 15; 4293-4298; <a href="https://doi.org/10.1021/bi00518a009">10.1021/bi00518a009</a></li>
<li>Kooistra, Dale A. and Richards, John H., el al. (1980) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150506-111329487">Binding Dynamics in Biological Systems. Interaction of MOPC-315 with ^(19)F Labelled Nitrophenyl Haptens</a>; Organic Magnetic Resonance; Vol. 13; No. 1; 1-8; <a href="https://doi.org/10.1002/mrc.1270130102">10.1002/mrc.1270130102</a></li>
<li>Moore, Kevin W. and Bachovchin, William W., el al. (1979) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-150734315">Hydrogen transfer in catalysis by adenosylcobalamin-dependent diol dehydratase</a>; Biochemistry; Vol. 18; No. 13; 2776-2782; <a href="https://doi.org/10.1021/bi00580a013">10.1021/bi00580a013</a></li>
<li>Moore, Kevin W. and Richards, John H. (1979) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-090534240">Stereospecificity and mechanism of adenosylcobalamin-dependent diol dehydratase. Catalysis and inactivation with meso- and dl-2,3-butanediols as substrates</a>; Biochemical and Biophysical Research Communications; Vol. 87; No. 4; 1052-1057; <a href="https://doi.org/10.1016/S0006-291X(79)80014-5">10.1016/S0006-291X(79)80014-5</a></li>
<li>Hunkapiller, Michael W. and Forgac, Michael D., el al. (1979) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-071027468">^(13)C NMR studies of the binding of soybean trypsin inhibitor to trypsin</a>; Biochemical and Biophysical Research Communications; Vol. 87; No. 1; 25-31; <a href="https://doi.org/10.1016/0006-291X(79)91642-5">10.1016/0006-291X(79)91642-5</a></li>
<li>Dill, Kilian and Satterlee, James D., el al. (1978) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-103739032">^(13)C nuclear magnetic resonance studies of the binding of isocyanides to various hemoglobins and myoglobins</a>; Biochemistry; Vol. 17; No. 20; 4291-4298; <a href="https://doi.org/10.1021/bi00613a028">10.1021/bi00613a028</a></li>
<li>Hardy, Richard R. and Richards, John H. (1978) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-111739006">Relation between structure and specificity of antibodies: nuclear magnetic resonance study of binding fluorine-19 labeled nitrophenyl haptens to myeloma immunoglobulins M315, M460, and X25</a>; Biochemistry; Vol. 17; No. 18; 3866-3871; <a href="https://doi.org/10.1021/bi00611a029">10.1021/bi00611a029</a></li>
<li>Goetze, Andrew M. and Richards, John H. (1978) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-153205407">Molecular studies of subspecificity differences among phosphorylcholine-binding mouse myeloma antibodies using ^(31)P nuclear magnetic resonance</a>; Biochemistry; Vol. 17; No. 9; 1733-1739; <a href="https://doi.org/10.1021/bi00602a023">10.1021/bi00602a023</a></li>
<li>Bachovchin, William W. and Moore, Kevin W., el al. (1978) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150501-152518245">Mechanism of action of adenosylcobalamin: hydrogen transfer in the inactivation of diol dehydratase by glycerol</a>; Biochemistry; Vol. 17; No. 11; 2218-2224; <a href="https://doi.org/10.1021/bi00604a031">10.1021/bi00604a031</a></li>
<li>Satterlee, James D. and Teintze, Martin, el al. (1978) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-141849896">Spectroscopic studies of the nature of ligand bonding in carbonmonoxyhemoglobins: evidence of a specific function for histidine-E7 from infrared and nuclear magnetic resonance intensities</a>; Biochemistry; Vol. 17; No. 8; 1456-1462; <a href="https://doi.org/10.1021/bi00601a015">10.1021/bi00601a015</a></li>
<li>Kooistra, Dale A. and Richards, John H. (1978) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150501-125733770">Magnetic resonance studies of the binding site interactions between ^(19)F-labeled nitrophenyl haptens and specific mouse myeloma immunoglobulin MOPC-315</a>; Biochemistry; Vol. 17; No. 2; 345-351; <a href="https://doi.org/10.1021/bi00595a024">10.1021/bi00595a024</a></li>
<li>Goetze, Andrew M. and Richards, John H. (1977) <a href="https://resolver.caltech.edu/CaltechAUTHORS:GOEpnas77">Structure-function relations in phosphorylcholine-binding mouse myeloma proteins</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 74; No. 5; 2109-2112</li>
<li>Bachovchin, William W. and Eagar, Robert G., Jr., el al. (1977) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-101355162">Mechanism of action of adenosylcobalamin: glycerol and other substrate analogs as substrates and inactivators for propanediol dehydratase - kinetics, stereospecificity, and mechanism</a>; Biochemistry; Vol. 16; No. 6; 1082-1092; <a href="https://doi.org/10.1021/bi00625a009">10.1021/bi00625a009</a></li>
<li>Moon, Richard B. and Dill, Kilian, el al. (1977) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-150820233">Magnetic resonance studies of the binding of ^(13)C-labeled carbon monoxide to myoglobins and hemoglobins containing modified hemes</a>; Biochemistry; Vol. 16; No. 2; 221-228; <a href="https://doi.org/10.1021/bi00621a010">10.1021/bi00621a010</a></li>
<li>Goetze, A. M. and Richards, J. H. (1977) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-104629036">Magnetic resonance studies of the binding site interactions between phosphorylcholine and specific mouse myeloma immunoglobulin</a>; Biochemistry; Vol. 16; No. 2; 228-232; <a href="https://doi.org/10.1021/bi00621a011">10.1021/bi00621a011</a></li>
<li>Hunkapiller, Michael W. and Forgac, Michael D., el al. (1976) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-094437203">Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer</a>; Biochemistry; Vol. 15; No. 25; 5581-5588; <a href="https://doi.org/10.1021/bi00670a024">10.1021/bi00670a024</a></li>
<li>Eagar, Robert G., Jr. and Bachovchin, William W., el al. (1975) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-134541144">Mechanism of action of adenosylcobalamin. 3-Fluoro-1,2-propanediol as substrate for propanediol dehydrase. Mechanistic implications</a>; Biochemistry; Vol. 14; No. 25; 5523-5528; <a href="https://doi.org/10.1021/bi00696a022">10.1021/bi00696a022</a></li>
<li>Hunkapiller, Michael W. and Smallcombe, Stephen H., el al. (1975) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-151434849">Mechanism of serine protease action. Ionization behavior of tetrahedral adduct between α-lytic protease and tripeptide aldehyde studied by carbon-13 magnetic resonance</a>; Organic Magnetic Resonance; Vol. 7; No. 6; 262-265; <a href="https://doi.org/10.1002/mrc.1270070604">10.1002/mrc.1270070604</a></li>
<li>Moon, Richard B. and Richards, John H. (1974) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-153247897">^(13)C magnetic resonance studies of the binding of carbon monoxide to various hemoglobins</a>; Biochemistry; Vol. 13; No. 17; 3437-3443; <a href="https://doi.org/10.1021/bi00714a003">10.1021/bi00714a003</a></li>
<li>Párkányi, Cyril and Richards, John H. (1974) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-143648839">Destructive Photooxidation of Tris(Dibenzoylmethanato)Iron(III)</a>; Journal of Coordination Chemistry; Vol. 4; No. 1; 41-45; <a href="https://doi.org/10.1080/00958977408075877">10.1080/00958977408075877</a></li>
<li>Moon, Richard B. and Nelson, Mark J., el al. (1974) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-081223308">^(13)C Magnetic Resonance Studies of Hemoglobin Carbamylation</a>; Physiological Chemistry and Physics; Vol. 6; No. 1; 31-40</li>
<li>Hunkapiller, Michael W. and Smallcombe, Stephen H., el al. (1973) <a href="https://resolver.caltech.edu/CaltechAUTHORS:HUNjbc73">Ionization behavior of the histidine residue in the catalytic triad of serine proteases</a>; Journal of Biological Chemistry; Vol. 248; No. 23; 8306-8308</li>
<li>Hunkapiller, Michael W. and Smallcombe, Stephen H., el al. (1973) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-104057052">Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease. Implications for the catalytic mechanism of serine proteases</a>; Biochemistry; Vol. 12; No. 23; 4732-4743; <a href="https://doi.org/10.1021/bi00747a028">10.1021/bi00747a028</a></li>
<li>Moon, Richard B. and Richards, John H. (1973) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20120814-130208418">Determination of Intracellular pH by ^(31)P Magnetic Resonance</a>; Journal of Biological Chemistry; Vol. 248; No. 20; 7276-7278</li>
<li>Dannenberg, J. J. and Levenberg, M. K., el al. (1973) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150427-153127795">The structure and bonding of ferrocenylcarbonium ions</a>; Tetrahedron; Vol. 29; No. 11; 1575-1584; <a href="https://doi.org/10.1016/S0040-4020(01)83399-8">10.1016/S0040-4020(01)83399-8</a></li>
<li>Moon, R. B. and Richards, J. H. (1972) <a href="https://resolver.caltech.edu/CaltechAUTHORS:MOOpnas72">Conformational studies of various hemoglobins by natural-abundance 13C NMR spectroscopy</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 69; No. 8; 2193-2197</li>
<li>Moon, Richard B. and Richards, John H. (1972) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-130344245">Nuclear magnetic resonance studies of ^(13)CO monoxide binding to various hemoglobins</a>; Journal of the American Chemical Society; Vol. 94; No. 14; 5093-5095; <a href="https://doi.org/10.1021/ja00769a058">10.1021/ja00769a058</a></li>
<li>Smallcombe, Stephen H. and Gammon, Kenneth L., el al. (1972) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-124735351">Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-tryptophan to α-chymotrypsin</a>; Journal of the American Chemical Society; Vol. 94; No. 13; 4581-4584; <a href="https://doi.org/10.1021/ja00768a028">10.1021/ja00768a028</a></li>
<li>Gammon, Kenneth L. and Smallcombe, Stephen H., el al. (1972) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-133401521">Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to α-chymotrypsin</a>; Journal of the American Chemical Society; Vol. 94; No. 13; 4573-4580; <a href="https://doi.org/10.1021/ja00768a027">10.1021/ja00768a027</a></li>
<li>Eagar, R. G., Jr. and Baltimore, B. G., el al. (1972) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-081550145">Mechanism of action of coenzyme B_(12). Hydrogen transfer in the isomerization of β-methylaspartate to glutamate</a>; Biochemistry; Vol. 11; No. 2; 253-264; <a href="https://doi.org/10.1021/bi00752a017">10.1021/bi00752a017</a></li>
<li>Jayme, Manfred and Richards, John H. (1971) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-085524057">Mechanism of action of coenzyme B_(12). Release of 5′-deoxyinosine on incubation of deoxyinosylcobalamin, 1,2-propanediol and propanediol dehydrase</a>; Biochemical and Biophysical Research Communications; Vol. 43; No. 6; 1329-1333; <a href="https://doi.org/10.1016/S0006-291X(71)80018-9">10.1016/S0006-291X(71)80018-9</a></li>
<li>Schmidt, Donald E., Jr. and Nigh, Wesley G., el al. (1969) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-094618091">Secondary isotope effects in dehydration of malic acid by fumarate hydratase</a>; Journal of the American Chemical Society; Vol. 91; No. 21; 5849-5854; <a href="https://doi.org/10.1021/ja01049a026">10.1021/ja01049a026</a></li>
<li>Nigh, Wesley G. and Richards, John H. (1969) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-084340544">Substrates for fumarate hydratase</a>; Journal of the American Chemical Society; Vol. 91; No. 21; 5847-5848; <a href="https://doi.org/10.1021/ja01049a025">10.1021/ja01049a025</a></li>
<li>Hall, David W. and Hill, E. Alexander, el al. (1968) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-142313160">Solvolysis of heteroannularly substituted methylferrocenylcarbinyl acetates</a>; Journal of the American Chemical Society; Vol. 90; No. 18; 4972-4976; <a href="https://doi.org/10.1021/ja01020a034">10.1021/ja01020a034</a></li>
<li>Werner, Helmut and Richards, John H. (1968) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-134522753">Reaction of nickelocene with diazoalkanes</a>; Journal of the American Chemical Society; Vol. 90; No. 18; 4976-4982; <a href="https://doi.org/10.1021/ja01020a035">10.1021/ja01020a035</a></li>
<li>Fisch, Michael H. and Richards, John H. (1968) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-153102777">Photoproducts form irradiation of lumisantonin in aprotic medium</a>; Journal of the American Chemical Society; Vol. 90; No. 6; 1553-1557; <a href="https://doi.org/10.1021/ja01008a027">10.1021/ja01008a027</a></li>
<li>Cais, Michael and Dannenberg, J. J., el al. (1966) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-092148166">Nuclear magnetic resonance spectra of ferrocenyl carbonium ions</a>; Tetrahedron Letters; Vol. 7; No. 15; 1695-1701; <a href="https://doi.org/10.1016/S0040-4039(01)99779-5">10.1016/S0040-4039(01)99779-5</a></li>
<li>Jones, Noel D. and Marsh, Richard E., el al. (1965) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-150500538">The crystal structure of α-keto-1,1'-trimethyleneferrocene</a>; Acta Crystallographica; Vol. 19; No. 3; 330-336; <a href="https://doi.org/10.1107/S0365110X65003407">10.1107/S0365110X65003407</a></li>
<li>Dannenberg, J. J. and Richards, J. H. (1965) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-082813986">Photosensitization by Ferrocene. Photochemistry of Higher Electronic Excited States</a>; Journal of the American Chemical Society; Vol. 87; No. 7; 1626-1627; <a href="https://doi.org/10.1021/ja01085a048">10.1021/ja01085a048</a></li>
<li>Ulery, H. E. and Richards, J. H. (1964) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150430-135625008">The Acid-Catalyzed Cyclization of Acyclic Dienes</a>; Journal of the American Chemical Society; Vol. 86; No. 15; 3113-3117; <a href="https://doi.org/10.1021/ja01069a028">10.1021/ja01069a028</a></li>
<li>Levenberg, Milton I. and Richards, J. H. (1964) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-145443614">An Analysis of the Nuclear Magnetic Resonance Spectra of Substituted Ferrocenes</a>; Journal of the American Chemical Society; Vol. 86; No. 13; 2634-2637; <a href="https://doi.org/10.1021/ja01067a023">10.1021/ja01067a023</a></li>
<li>Richards, J. H. and Walker, S. (1964) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-091225034">Mesomeric and electromeric factors in the mononitronaphthylamines</a>; Tetrahedron; Vol. 20; No. 4; 841-853; <a href="https://doi.org/10.1016/S0040-4020(01)98416-9">10.1016/S0040-4020(01)98416-9</a></li>
<li>Beach, William F. and Richards, John H. (1963) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-144350665">The Structure and Biosynthesis of Nidulin</a>; Journal of Organic Chemistry; Vol. 28; No. 10; 2746-2751; <a href="https://doi.org/10.1021/jo01045a061">10.1021/jo01045a061</a></li>
<li>Fisch, M. H. and Richards, J. H. (1963) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-140626111">The Mechanism of the Photoconversion of Santonin</a>; Journal of the American Chemical Society; Vol. 85; No. 19; 3029-3030; <a href="https://doi.org/10.1021/ja00902a038">10.1021/ja00902a038</a></li>
<li>Hall, David W. and Richards, John H. (1963) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-161554242">The Acetylation of Some Substituted Ferrocenes</a>; Journal of Organic Chemistry; Vol. 28; No. 6; 1547-1554; <a href="https://doi.org/10.1021/jo01041a026">10.1021/jo01041a026</a></li>
<li>Richards, John H. (1963) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150506-092654869">Role of Acetate in Biosynthesis</a>; Antimicrobial Agents and Chemotherapy; Vol. 161; 349-351</li>
<li>Mock, William and Richards, John H. (1962) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150505-123958200">The Synthesis of Bridged Ferrocene Derivatives with Functional Groups on the β-Carbon of the Bridge</a>; Journal of Organic Chemistry; Vol. 27; No. 11; 4050-4051; <a href="https://doi.org/10.1021/jo01058a504">10.1021/jo01058a504</a></li>
<li>Hill, E. Alexander and Richards, John H. (1961) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-115105989">Carbonium Ion Stabilization by Metallocene Nuclei. III. Evidence for Metal Participation</a>; Journal of the American Chemical Society; Vol. 83; No. 20; 4216-4221; <a href="https://doi.org/10.1021/ja01481a029">10.1021/ja01481a029</a></li>
<li>Hill, E. Alexander and Richards, John H. (1961) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150429-085400147">Carbonium Ion Stabilization by Metallocene Nuclei. II. α-Metallocenylcarbonium Ions</a>; Journal of the American Chemical Society; Vol. 83; No. 18; 3840-3846; <a href="https://doi.org/10.1021/ja01479a025">10.1021/ja01479a025</a></li>
<li>Beach, W. F. and Richards, J. H. (1961) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150504-110641683">The Nature of the Alkyl Groups in Nidulin</a>; Journal of Organic Chemistry; Vol. 26; No. 8; 3011-3012; <a href="https://doi.org/10.1021/jo01066a622">10.1021/jo01066a622</a></li>
<li>Beach, W. F. and Richards, J. H. (1961) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150501-163652322">The Structure of Nidulin</a>; Journal of Organic Chemistry; Vol. 26; No. 4; 1339-1340; <a href="https://doi.org/10.1021/jo01063a073">10.1021/jo01063a073</a></li>
<li>Richards, John H. and Beach, William F. (1961) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-142630801">Long Range Splittings in the NMR Spectra of Isomeric 2-Bromo-2-butenes</a>; Journal of Organic Chemistry; Vol. 26; No. 2; 623-624; <a href="https://doi.org/10.1021/jo01061a624">10.1021/jo01061a624</a></li>
<li>Carter, R. E. and Richards, J. H. (1961) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-141801341">The biogenesis of phenazine pigments</a>; Journal of the American Chemical Society; Vol. 83; No. 2; 495-496; <a href="https://doi.org/10.1021/ja01463a063">10.1021/ja01463a063</a></li>
<li>Fraenkel, Gideon and Carter, Robert E., el al. (1960) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150501-164555658">Chemical Shifts in C_5H_5^-, C_6H_6 and C_7H_7^+; Chemical Shifts and π-Electron Densities</a>; Journal of the American Chemical Society; Vol. 82; No. 22; 5846-5850; <a href="https://doi.org/10.1021/ja01507a020">10.1021/ja01507a020</a></li>
<li>Ferretti, L. D. and Richards, J. H. (1960) <a href="https://resolver.caltech.edu/CaltechAUTHORS:FERpnas60">The biogenesis of the mold tropolones</a>; Proceedings of the National Academy of Sciences of the United States of America; Vol. 46; No. 11; 1438-1444; <a href="https://doi.org/10.1073/pnas.46.11.1438">10.1073/pnas.46.11.1438</a></li>
<li>Curphey, T. J. and Santer, J. O., el al. (1960) <a href="https://resolver.caltech.edu/CaltechAUTHORS:20150428-140300077">Protonation of metallocenes by strong acids. Structure of the cation</a>; Journal of the American Chemical Society; Vol. 82; No. 19; 5249-5250; <a href="https://doi.org/10.1021/ja01504a062">10.1021/ja01504a062</a></li>
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