Richards, John H.

Combined from CaltechAUTHORS

• Warren, Jeffrey J. and Lancaster, Kyle M., et el. (2012) Inner- and outer-sphere metal coordination in blue copper proteins; Journal of Inorganic Biochemistry; Vol. 115; 119-126; PMCID PMC3434318; 10.1016/j.jinorgbio.2012.05.002
• Lancaster, Kyle M. and Zaballa, María-Eugenia, et el. (2012) Outer-Sphere Contributions to the Electronic Structure of Type Zero Copper Proteins; Journal of the American Chemical Society; Vol. 134; No. 19; 8241-8253; PMCID PMC4794991; 10.1021/ja302190r
• Potapov, Alexey and Lancaster, Kyle M., et el. (2012) Spin Delocalization Over Type Zero Copper; Inorganic Chemistry; Vol. 51; No. 7; 4066-4075; PMCID PMC3322426; 10.1021/ic202336m
• Lancaster, Kyle M. and Farver, Ole, et el. (2011) Electron Transfer Reactivity of Type Zero Pseudomonas aeruginosa Azurin; Journal of the American Chemical Society; Vol. 133; No. 13; 4865-4873; PMCID PMC3607328; 10.1021/ja1093919
• Yokoyama, K. and Nakamura, N., et el. (2010) Electron tunneling through mutant azurins on mixed SAM gold electrodes
• Lancaster, Kyle M. and Sproules, Stephen, et el. (2010) Outer-Sphere Effects on Reduction Potentials of Copper Sites in Proteins: The Curious Case of High Potential Type 2 C112D/M121E Pseudomonas aeruginosa Azurin; Journal of the American Chemical Society; Vol. 132; No. 41; 14590-14595; PMCID PMC3375907; 10.1021/ja105731x
• Lancaster, Kyle M. and George, Serena DeBeer, et el. (2009) Type-zero copper proteins; Nature Chemistry; Vol. 1; No. 9; 711-715; PMCID PMC2841405; 10.1038/NCHEM.412
• Lancaster, Kyle M. and Yokoyama, Keiko, et el. (2009) High-Potential C112D/M121X (X = M, E, H, L) Pseudomonas aeruginosa Azurins; Inorganic Chemistry; Vol. 48; No. 4; 1278-1280; PMCID PMC2765487; 10.1021/ic802322e
• Shih, Crystal and Museth, Anna Katrine, et el. (2008) Tryptophan-Accelerated Electron Flow Through Proteins; Science; Vol. 320; No. 5884; 1760-1762; 10.1126/science.1158241
• Yokoyama, Keiko and Leigh, Brian S., et el. (2008) Electron Tunneling through Pseudomonas aeruginosa Azurins on SAM Gold Electrodes; Inorganica Chimica Acta; Vol. 361; No. 4; 1095-1099; PMCID PMC2390814; 10.1016/j.ica.2007.08.022
• Kim, Judy E. and Arjara, Gitrada, et el. (2006) Probing folded and unfolded states of outer membrane protein a with steady-state and time-resolved tryptophan fluorescence; Journal of Physical Chemistry B; Vol. 110; No. 35; 17656-62; PMCID PMC2519049; 10.1021/jp061991r
• Blanco-Rodríguez, Ana María and Busby, Michael, et el. (2006) Excited-State Dynamics of Structurally Characterized [Re^I(CO)_3(phen)(HisX)]^+ (X = 83, 109) Pseudomonas aeruginosa Azurins in Aqueous Solution; Journal of the American Chemical Society; Vol. 128; No. 13; 4365-4370; 10.1021/ja057451+
• Blanco-Rodríguez, Ana María and Busby, Michael, et el. (2006) Excited-State Dynamics of Structurally Characterized [Re^I(CO)_3(phen)(HisX)]^+(X = 83, 109) Pseudomonas aeruginosa Azurins in Aqueous Solution; Journal of the American Chemical Society; Vol. 128; No. 13; 4365-4370; 10.1021/ja057451+
• Fujita, Kyoko and Nakamura, Nobufumi, et el. (2004) 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; Journal of the American Chemical Society; Vol. 126; No. 43; 13954-61; 10.1021/ja047875o
• Niki, Katsumi and Hardy, W. Reef, et el. (2003) Coupling to Lysine-13 Promotes Electron Tunneling through Carboxylate-Terminated Alkanethiol Self-Assembled Monolayers to Cytochrome c; Journal of Physical Chemistry B; Vol. 107; No. 37; 9947-9949; 10.1021/jp035392l
• McGuirl, Michele A. and Lee, Jennifer C., et el. (2003) Cloning, heterologous expression, and characterization of recombinant class II cytochromes c from Rhodopseudomonas palustris; Biochimica et Biophysica Acta - General Subjects; Vol. 1619; No. 1; 23-8; 10.1016/S0304-4165(02)00437-3
• Machczynski, Michael C. and Gray, Harry B., et el. (2002) An outer-sphere hydrogen-bond network constrains copper coordination in blue proteins; Journal of Inorganic Biochemistry; Vol. 88; No. 3-4; 375-80; 10.1016/S0162-0134(02)00364-1
• Fernández, Claudio O. and Cricco, Julia A., et el. (2001) Axial Ligand Modulation of the Electronic Structures of Binuclear Copper Sites:  Analysis of Paramagnetic ^1H NMR Spectra of Met160Gln Cu_A; Journal of the American Chemical Society; Vol. 123; No. 47; 11678-11685; 10.1021/ja0162515
• Slutter, Claire E. and Gromov, Igor, et el. (2001) Pulsed EPR/ENDOR Characterization of Perturbations of the Cu_A Center Ground State by Axial Methionine Ligand Mutations; Journal of the American Chemical Society; Vol. 123; No. 22; 5325-5336; 10.1021/ja003924v
• Di Bilio, Angel J. and Crane, Brian R., et el. (2001) Properties of Photogenerated Tryptophan and Tyrosyl Radicals in Structurally Characterized Proteins Containing Rhenium(I) Tricarbonyl Diimines; Journal of the American Chemical Society; Vol. 123; No. 13; 3181-3182; 10.1021/ja0043183
• Webb, M. Adam and Kiser, Cynthia N., et el. (2000) Resonance Raman Spectroscopy of Met121Glu Azurin; Journal of Physical Chemistry B; Vol. 104; No. 46; 10915-10920; 10.1021/jp000832j
• Winkler, Jay R. and Di Bilio, Angel J., et el. (1999) Electron tunneling in biological molecules; Pure and Applied Chemistry; Vol. 71; No. 9; 1753-1764; 10.1351/pac199971091753
• Slutter, Claire E. and Gromov, Igor, et el. (1999) Mutations of the Weak Axial Ligand in the Thermus CuA Center Modulates Its Electronic Structure; Journal of the American Chemical Society; Vol. 121; No. 21; 5077-5078; 10.1021/ja984361e
• DeBeer, Serena and Kiser, Cynthia N., et el. (1999) X-ray Absorption Spectra of the Oxidized and Reduced Forms of C112D Azurin from Pseudomonas aeruginosa; Inorganic Chemistry; Vol. 38; No. 3; 433-438; 10.1021/ic9804622
• Regan, J. J. and Di Bilio, A. J., et el. (1998) Electron tunneling in Ru-modified His46Asp azurin. Coupling through the Cu ligands; Inorganica Chimica Acta; Vol. 275-276; No. 1-2; 470-480; 10.1016/S0020-1693(98)00066-8
• Vila, A. J. and Ramirez, B. E., et el. (1997) Paramagnetic NMR Spectroscopy of Cobalt(II) and Copper(II) Derivatives of Pseudomonas aeruginosa His46Asp Azurin; Inorganic Chemistry; Vol. 36; No. 20; 4567-4570; 10.1021/ic9703282
• Faham, Salem and Mizoguchi, Tadashi J., et el. (1997) Role of the active-site cysteine of Pseudomonas aeruginosa azurin. Crystal structure analysis of the Cu^(II(Cys112Asp) protein; Journal of Biological Inorganic Chemistry; Vol. 2; No. 4; 464-469; 10.1007/s007750050157
• Vanhove, Marc and Guillaume, Gilliane, et el. (1997) Kinetic and thermodynamic consequences of the removal of the Cys-77–Cys-123 disulphide bond for the folding of TEM-1 β-lactamase; Biochemical Journal; Vol. 321; No. Part 2; 413-417
• Immoos, Chad and Hill, Michael G., et el. (1996) Electrochemistry of the Cu_A domain of Thermus thermophilus cytochrome ba _3; Journal of Biological Inorganic Chemistry; Vol. 1; No. 6; 529-531; 10.1007/s007750050088
• Bertini, Ivano and Bren, Kara L., et el. (1996) The Cu_A Center of a Soluble Domain from Thermus Cytochrome ba_3. An NMR Investigation of the Paramagnetic Protein; Journal of the American Chemical Society; Vol. 118; No. 46; 11658-11659; 10.1021/ja9621410
• McCleskey, T. Mark and Mizoguchi, Tadashi J., et el. (1996) Electronic Spectroscopy of Gold(I) Pseudomonasaeruginosa Azurin Derivatives; Inorganic Chemistry; Vol. 35; No. 11; 3434-3435; 10.1021/ic951055i
• Slutter, Claire E. and Sanders, Donita, et el. (1996) Water-Soluble, Recombinant Cu_A-Domain of the Cytochrome ba_3 Subunit II from Thermus thermophilus; Biochemistry; Vol. 35; No. 11; 3387-3395; 10.1021/bi9525839
• Slutter, Claire E. and Langen, Ralf, et el. (1996) Electron-transfer studies with the CuA domain of Thermus thermophilus cytochrome ba_3; Inorganica Chimica Acta; Vol. 243; No. 1-2; 141-145; 10.1016/0020-1693(95)04901-0
• Hay, Michael and Richards, John H., et el. (1996) Construction and characterization of an azurin analog for the purple copper site in cytochrome c oxidase; Proceedings of the National Academy of Sciences of the United States of America; Vol. 93; No. 1; 461-464; PMCID PMC40258; 10.1073/pnas.93.1.461
• Langen, Ralf and Chang, I-Jy, et el. (1995) Electron Tunneling in Proteins: Coupling Through a β Strand; Science; Vol. 268; No. 5218; 1733-1735; 10.1126/science.7792598
• Piccioli, Mario and Luchinat, Claudio, et el. (1995) Paramagnetic NMR spectroscopy and coordination structure of cobalt(II) Cys112Asp azurin; Inorganic Chemistry; Vol. 34; No. 3; 737-742; 10.1021/ic00107a027
• Casimiro, Danilo R. and Richards, John H., et el. (1993) Electron Transfer in Ruthenium-Modified Cytochromes c. σ-Tunneling Pathways through Aromatic Residues; Journal of Physical Chemistry; Vol. 97; No. 50; 13073-13077; 10.1021/j100152a007
• Lu, Yi and Casimiro, Danilo R., et el. (1993) Structurally engineered cytochromes with unusual ligand-binding properties: Expression of Saccharomyces cerevisiae Met-80 --> Ala iso-1-cytochrome c; Proceedings of the National Academy of Sciences of the United States of America; Vol. 90; No. 24; 11456-11459; PMCID PMC48002
• Germanas, Juris P. and Di Bilio, Angel J., et el. (1993) Site saturation of the histidine-46 position in Pseudomonas aeruginosa azurin: Characterization of the His46Asp copper and cobalt proteins; Biochemistry; Vol. 32; No. 30; 7698-7702; 10.1021/bi00081a014
• Casimiro, Danilo R. and Wong, Luet-L., et el. (1993) Electron Transfer in Ruthenium/Zinc Porphyrin Derivatives of Recombinant Human Myoglobins. Analysis of Tunneling Pathways in Myoglobin and Cytochrome c; Journal of the American Chemical Society; Vol. 115; No. 4; 1485-1489; 10.1021/ja00057a037
• Mizoguchi, Tadashi J. and Di Bilio, Angel J., et el. (1992) Blue to type 2 binding. Copper(II) and cobalt(II) derivatives of a Cys112Asp mutant of Pseudomonas aeruginosa azurin; Journal of the American Chemical Society; Vol. 114; No. 25; 10076-10078; 10.1021/ja00051a059
• Tomich, John M. and Richards, John H. (1992) Synthetic metalloproteins; ISBN 9789072199126; Peptides: Chemistry and Biology; 431-432
• Casimiro, Danilo R. and Winkler, Jay R., et el. (1992) Long-Range Electron Transfer in Ruthenium-Modified Cytochromes c. σ-Tunneling Pathways through Aromatic Residues; ISBN 9780792320913; Research in Photosynthesis; 829-832
• Smith, Eugene T. and Tomich, John M., et el. (1991) A totally synthetic histidine-2 ferredoxin: thermal stability and redox properties; Biochemistry; Vol. 30; No. 50; 11669-11676; 10.1021/bi00114a009
• Chang, Thomas K. and Iverson, Sheila A., et el. (1991) Gene Synthesis, Expression, and Mutagenesis of the Blue Copper Proteins Azurin and Plastocyanin; Proceedings of the National Academy of Sciences of the United States of America; Vol. 88; No. 4; 1325-1329; PMCID PMC51010; 10.1073/pnas.88.4.1325
• Smith, Eugene T. and Feinberg, Benjamin A., et el. (1991) Physical characterization of a totally synthetic 2[4Fe-4S] clostridial ferredoxin; Journal of the American Chemical Society; Vol. 113; No. 2; 688-689; 10.1021/ja00002a055
• Chang, Yie-Hwa and Labgold, Marc R., et el. (1990) Altering Enzymatic Activity: Recruitment of Carboxypeptidase Activity into an RTEM β-Lactamase/Penicillin-Binding Protein 5 Chimera; Proceedings of the National Academy of Sciences of the United States of America; Vol. 87; No. 7; 2823-2827; PMCID PMC53783; 10.1073/pnas.87.7.2823
• Labgold, Marc R. and Chang, Yie-Hwa, et el. (1990) Catalysis by Chimeric Proteins: Conversion of a β-lactamase to a D,D-Carboxypeptidase; ISBN 978-0-12-721955-4; Current Research in Protein Chemistry; 489-497; 10.1016/B978-0-12-721955-4.50051-8
• Bowler, Bruce E. and Meade, Thomas J., et el. (1989) Long-range electron transfer in structurally engineered pentaammineruthenium (histidine-62) cytochrome c; Journal of the American Chemical Society; Vol. 111; No. 23; 8757-8759; 10.1021/ja00205a049
• Hawke, David H. and Meister, Suzanne M., et el. (1989) Studies on C-Terminal Analysis; ISBN 0-12-682000-7; Techniques in Protein Chemistry; 59-66; 10.1016/B978-0-12-682001-0.50013-0
• Healey, William J. and Labgold, Marc R., et el. (1989) Substrate specificities in class A β-lactamases: Preference for penams vs. cephams. The role of residues 237; Proteins; Vol. 6; No. 3; 275-283; 10.1002/prot.340060310
• Tomich, John M. and Carson, L. Wulf, et el. (1988) Prevention of Aggregation of Synthetic Membrane-Spanning Peptides by Addition of Detergent; Analytical Biochemistry; Vol. 174; No. 1; 197-203; 10.1016/0003-2697(88)90535-0
• Roise, David and Theiler, Franziska, et el. (1988) Amphiphilicity is essential for mitochondrial presequence function; EMBO Journal; Vol. 7; No. 3; 649-653; PMCID PMC454369; 10.1002/j.1460-2075.1988.tb02859.x
• Foster, Patricia L. and Dalbadie-McFarland, Gloria, et el. (1987) 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; Journal of Bacteriology; Vol. 169; No. 6; 2476-2481; PMCID PMC212096
• Carroll, Steven S. and Richards, John H. (1987) Progress Toward the Rational Study of Enzyme Structure-Function Relationships; Annual Reports in Medicinal Chemistry; Vol. 22; 293-301
• Schultz, Steve C. and Dalbadie-McFarland, Gloria, et el. (1987) Stability of wild-type and mutant RTEM-1 β-lactamases: Effect of the disulfide bond; Proteins; Vol. 2; No. 4; 290-297; 10.1002/prot.340020405
• Merchant, Sabeeha and Bogorad, Lawrence, et el. (1986) Molecular Characterization of Chlamydomonas Reinhardtii, ac-208: A Plastocyanin-Less Mutant; ISBN 9024734533; Progress in Photosynthesis Research; 663-666; 10.1007/978-94-017-0519-6_137
• Schultz, Steve C. and Richards, John H. (1986) Site-saturation studies of β-lactamase: Production and characterization of mutant β-lactamases with all possible amino acid substitutions at residue 71; Proceedings of the National Academy of Sciences of the United States of America; Vol. 83; No. 6; 1588-1592; PMCID PMC323128; 10.1073/pnas.83.6.1588
• Dalbadie-McFarland, Gloria and Neitzel, James J., et el. (1986) Active-site mutants of β-lactamase: use of an inactive double mutant to study requirements for catalysis; Biochemistry; Vol. 25; No. 2; 332-338; 10.1021/bi00350a008
• Roise, David and Horvath, Suzanna J., et el. (1986) A chemically synthesized pre-sequence of an imported mitochondrial protein can form an amphiphilic helix and perturb natural and artificial phospholipid bilayers; EMBO Journal; Vol. 5; No. 6; 1327-1334; PMCID PMC1166944
• Lad, P. M. and Glovsky, M. M., et el. (1985) Regulation of human neutrophil guanylate cyclase by metal ions, free radicals and the muscarinic cholinergic receptor; Molecular Immunology; Vol. 22; No. 7; 731-739; 10.1016/0161-5890(85)90138-5
• Dalbadie-McFarland, G. and Neitzel, J., et el. (1984) Studies of Protein Function by Various Mutagenic Strategies: β-Lactamase; Annals of the New York Academy of Sciences; Vol. 434; 232-238; 10.1111/j.1749-6632.1984.tb29833.x
• Lad, P. M. and Glovsky, M. M., et el. (1984) Identification of receptor regulatory proteins, membrane glycoproteins, and functional characteristics of adenylate cyclase in vesicles derived from the human neutrophil; Molecular Immunology; Vol. 21; No. 7; 627-639; 10.1016/0161-5890(84)90048-8
• Dalbadie-McFarland, G. and Riggs, A. D., et el. (1984) Directed mutagenesis as a technique to study protein function: application to β-lactamase; Biochemical Society Transactions; Vol. 12; No. 2; 226-228; 10.1042/bst0120226
• Lad, Pramod M. and Glovsky, M. Michael, et el. (1984) The β-adrenergic receptor in the human neutrophil plasma membrane: receptor-cyclase uncoupling is associated with amplified GTP activation; Journal of Immunology; Vol. 132; No. 3; 1466-1471
• Goers, John W. and Glovsky, M. Michael, et el. (1984) Studies on C3a_(hu) Binding to Human Eosinophils: Characterization of Binding; International Archives of Allergy and Applied Immunology; Vol. 74; No. 2; 147-151; 10.1159/000233535
• Perkins, T. and Satterlee, J. D., et el. (1983) Mechanism of T_1 relaxation in ^(13)CO complexed to an iron porphyrin: implications for CO bonding in heme proteins; Journal of the American Chemical Society; Vol. 105; No. 5; 1350-1354; 10.1021/ja00343a047
• Dalbadie-McFarland, Gloria and Richards, John H. (1983) Chapter 24. In Vitro Mutagenesis:Relationships in Proteins Powerful New Techniques for Studying Structure-Function Relationships in Proteins; ISBN 978-0-12-040518-3; Annual Reports in Medicinal Chemistry; 237-245; 10.1016/S0065-7743(08)60779-4
• Dalbadie-McFarland, G. and Cohen, L. W., et el. (1982) Oligonucleotide-Directed Mutagenesis as a General and Powerful Method for Studies of Protein Function; Proceedings of the National Academy of Sciences of the United States of America; Vol. 79; No. 21; 6409-6413
• McGee, Dennis E. and Carroll, Steven S., et el. (1982) Diol dehydratase: N-terminal amino acid sequences and subunit stoichiometry; Biochemical and Biophysical Research Communications; Vol. 108; No. 2; 547-551; 10.1016/0006-291X(82)90863-4
• Richards, J. H. and Teeri, J. A. (1982) Re-evaluation of proposed C_4 photosynthetic characteristics in the genus Larix; Physiologia Plantarum; Vol. 55; No. 2; 117-120; 10.1111/j.1399-3054.1982.tb02273.x
• Alder, George and Richards, John H. (1982) The Effect of DPG and IHP on the Relative Thermodynamic Affinity for CO of the Subunits of Rabbit Hemoglobin
• Cohen, L. and Molin, C., et el. (1982) Proteins to Order Use of Synthetic DNA to Generate Site-Specific Mutations
• Bachovchin, William W. and Kaiser, Robert, et el. (1981) 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; Proceedings of the National Academy of Sciences of the United States of America; Vol. 78; No. 12; 7323-7326
• McGee, Dennis E. and Richards, John H. (1981) Purification and subunit characterization of propanediol dehydratase, a membrane-associated enzyme; Biochemistry; Vol. 20; No. 15; 4293-4298; 10.1021/bi00518a009
• Kooistra, Dale A. and Richards, John H., et el. (1980) Binding Dynamics in Biological Systems. Interaction of MOPC-315 with ^(19)F Labelled Nitrophenyl Haptens; Organic Magnetic Resonance; Vol. 13; No. 1; 1-8; 10.1002/mrc.1270130102
• Moore, Kevin W. and Bachovchin, William W., et el. (1979) Hydrogen transfer in catalysis by adenosylcobalamin-dependent diol dehydratase; Biochemistry; Vol. 18; No. 13; 2776-2782; 10.1021/bi00580a013
• Moore, Kevin W. and Richards, John H. (1979) Stereospecificity and mechanism of adenosylcobalamin-dependent diol dehydratase. Catalysis and inactivation with meso- and dl-2,3-butanediols as substrates; Biochemical and Biophysical Research Communications; Vol. 87; No. 4; 1052-1057; 10.1016/S0006-291X(79)80014-5
• Hunkapiller, Michael W. and Forgac, Michael D., et el. (1979) ^(13)C NMR studies of the binding of soybean trypsin inhibitor to trypsin; Biochemical and Biophysical Research Communications; Vol. 87; No. 1; 25-31; 10.1016/0006-291X(79)91642-5
• Dill, Kilian and Satterlee, James D., et el. (1978) ^(13)C nuclear magnetic resonance studies of the binding of isocyanides to various hemoglobins and myoglobins; Biochemistry; Vol. 17; No. 20; 4291-4298; 10.1021/bi00613a028
• Hardy, Richard R. and Richards, John H. (1978) 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; Biochemistry; Vol. 17; No. 18; 3866-3871; 10.1021/bi00611a029
• Goetze, Andrew M. and Richards, John H. (1978) Molecular studies of subspecificity differences among phosphorylcholine-binding mouse myeloma antibodies using ^(31)P nuclear magnetic resonance; Biochemistry; Vol. 17; No. 9; 1733-1739; 10.1021/bi00602a023
• Bachovchin, William W. and Moore, Kevin W., et el. (1978) Mechanism of action of adenosylcobalamin: hydrogen transfer in the inactivation of diol dehydratase by glycerol; Biochemistry; Vol. 17; No. 11; 2218-2224; 10.1021/bi00604a031
• Satterlee, James D. and Teintze, Martin, et el. (1978) 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; Biochemistry; Vol. 17; No. 8; 1456-1462; 10.1021/bi00601a015
• Kooistra, Dale A. and Richards, John H. (1978) Magnetic resonance studies of the binding site interactions between ^(19)F-labeled nitrophenyl haptens and specific mouse myeloma immunoglobulin MOPC-315; Biochemistry; Vol. 17; No. 2; 345-351; 10.1021/bi00595a024
• Goetze, Andrew M. and Richards, John H. (1977) Structure-function relations in phosphorylcholine-binding mouse myeloma proteins; Proceedings of the National Academy of Sciences of the United States of America; Vol. 74; No. 5; 2109-2112
• Bachovchin, William W. and Eagar, Robert G., Jr., et el. (1977) Mechanism of action of adenosylcobalamin: glycerol and other substrate analogs as substrates and inactivators for propanediol dehydratase - kinetics, stereospecificity, and mechanism; Biochemistry; Vol. 16; No. 6; 1082-1092; 10.1021/bi00625a009
• Moon, Richard B. and Dill, Kilian, et el. (1977) Magnetic resonance studies of the binding of ^(13)C-labeled carbon monoxide to myoglobins and hemoglobins containing modified hemes; Biochemistry; Vol. 16; No. 2; 221-228; 10.1021/bi00621a010
• Goetze, A. M. and Richards, J. H. (1977) Magnetic resonance studies of the binding site interactions between phosphorylcholine and specific mouse myeloma immunoglobulin; Biochemistry; Vol. 16; No. 2; 228-232; 10.1021/bi00621a011
• Hunkapiller, Michael W. and Forgac, Michael D., et el. (1976) Mechanism of action of serine proteases: tetrahedral intermediate and concerted proton transfer; Biochemistry; Vol. 15; No. 25; 5581-5588; 10.1021/bi00670a024
• Eagar, Robert G., Jr. and Bachovchin, William W., et el. (1975) Mechanism of action of adenosylcobalamin. 3-Fluoro-1,2-propanediol as substrate for propanediol dehydrase. Mechanistic implications; Biochemistry; Vol. 14; No. 25; 5523-5528; 10.1021/bi00696a022
• Hunkapiller, Michael W. and Smallcombe, Stephen H., et el. (1975) Mechanism of serine protease action. Ionization behavior of tetrahedral adduct between α-lytic protease and tripeptide aldehyde studied by carbon-13 magnetic resonance; Organic Magnetic Resonance; Vol. 7; No. 6; 262-265; 10.1002/mrc.1270070604
• Moon, Richard B. and Richards, John H. (1974) ^(13)C magnetic resonance studies of the binding of carbon monoxide to various hemoglobins; Biochemistry; Vol. 13; No. 17; 3437-3443; 10.1021/bi00714a003
• Moon, Richard B. and Nelson, Mark J., et el. (1974) ^(13)C Magnetic Resonance Studies of Hemoglobin Carbamylation; Physiological Chemistry and Physics; Vol. 6; No. 1; 31-40
• Párkányi, Cyril and Richards, John H. (1974) Destructive Photooxidation of Tris(Dibenzoylmethanato)Iron(III); Journal of Coordination Chemistry; Vol. 4; No. 1; 41-45; 10.1080/00958977408075877
• Hunkapiller, Michael W. and Smallcombe, Stephen H., et el. (1973) Ionization behavior of the histidine residue in the catalytic triad of serine proteases; Journal of Biological Chemistry; Vol. 248; No. 23; 8306-8308
• Hunkapiller, Michael W. and Smallcombe, Stephen H., et el. (1973) Carbon nuclear magnetic resonance studies of the histidine residue in α-lytic protease. Implications for the catalytic mechanism of serine proteases; Biochemistry; Vol. 12; No. 23; 4732-4743; 10.1021/bi00747a028
• Moon, Richard B. and Richards, John H. (1973) Determination of Intracellular pH by ^(31)P Magnetic Resonance; Journal of Biological Chemistry; Vol. 248; No. 20; 7276-7278
• Dannenberg, J. J. and Levenberg, M. K., et el. (1973) The structure and bonding of ferrocenylcarbonium ions; Tetrahedron; Vol. 29; No. 11; 1575-1584; 10.1016/S0040-4020(01)83399-8
• Moon, R. B. and Richards, J. H. (1972) Conformational studies of various hemoglobins by natural-abundance 13C NMR spectroscopy; Proceedings of the National Academy of Sciences of the United States of America; Vol. 69; No. 8; 2193-2197
• Moon, Richard B. and Richards, John H. (1972) Nuclear magnetic resonance studies of ^(13)CO monoxide binding to various hemoglobins; Journal of the American Chemical Society; Vol. 94; No. 14; 5093-5095; 10.1021/ja00769a058
• Smallcombe, Stephen H. and Gammon, Kenneth L., et el. (1972) Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-tryptophan to α-chymotrypsin; Journal of the American Chemical Society; Vol. 94; No. 13; 4581-4584; 10.1021/ja00768a028
• Gammon, Kenneth L. and Smallcombe, Stephen H., et el. (1972) Magnetic resonance studies of protein-small molecule interactions. Binding of N-trifluoroacetyl-D-(and L-)-p-fluorophenylalanine to α-chymotrypsin; Journal of the American Chemical Society; Vol. 94; No. 13; 4573-4580; 10.1021/ja00768a027
• Eagar, R. G., Jr. and Baltimore, B. G., et el. (1972) Mechanism of action of coenzyme B_(12). Hydrogen transfer in the isomerization of β-methylaspartate to glutamate; Biochemistry; Vol. 11; No. 2; 253-264; 10.1021/bi00752a017
• Jayme, Manfred and Richards, John H. (1971) Mechanism of action of coenzyme B_(12). Release of 5′-deoxyinosine on incubation of deoxyinosylcobalamin, 1,2-propanediol and propanediol dehydrase; Biochemical and Biophysical Research Communications; Vol. 43; No. 6; 1329-1333; 10.1016/S0006-291X(71)80018-9
• Richards, J. H. (1970) Kinetic Isotope Effects in Enzymic Reactions; ISBN 978-0-12-122702-9; The Enzymes; 321-333; 10.1016/S1874-6047(08)60185-7
• Schmidt, Donald E., Jr. and Nigh, Wesley G., et el. (1969) Secondary isotope effects in dehydration of malic acid by fumarate hydratase; Journal of the American Chemical Society; Vol. 91; No. 21; 5849-5854; 10.1021/ja01049a026
• Nigh, Wesley G. and Richards, John H. (1969) Substrates for fumarate hydratase; Journal of the American Chemical Society; Vol. 91; No. 21; 5847-5848; 10.1021/ja01049a025
• Hall, David W. and Hill, E. Alexander, et el. (1968) Solvolysis of heteroannularly substituted methylferrocenylcarbinyl acetates; Journal of the American Chemical Society; Vol. 90; No. 18; 4972-4976; 10.1021/ja01020a034
• Werner, Helmut and Richards, John H. (1968) Reaction of nickelocene with diazoalkanes; Journal of the American Chemical Society; Vol. 90; No. 18; 4976-4982; 10.1021/ja01020a035
• Fisch, Michael H. and Richards, John H. (1968) Photoproducts form irradiation of lumisantonin in aprotic medium; Journal of the American Chemical Society; Vol. 90; No. 6; 1553-1557; 10.1021/ja01008a027
• Cais, Michael and Dannenberg, J. J., et el. (1966) Nuclear magnetic resonance spectra of ferrocenyl carbonium ions; Tetrahedron Letters; Vol. 7; No. 15; 1695-1701; 10.1016/S0040-4039(01)99779-5
• Jones, Noel D. and Marsh, Richard E., et el. (1965) The crystal structure of α-keto-1,1'-trimethyleneferrocene; Acta Crystallographica; Vol. 19; No. 3; 330-336; 10.1107/S0365110X65003407
• Dannenberg, J. J. and Richards, J. H. (1965) Photosensitization by Ferrocene. Photochemistry of Higher Electronic Excited States; Journal of the American Chemical Society; Vol. 87; No. 7; 1626-1627; 10.1021/ja01085a048
• Richards, John H. (1964) Reactions Of Metallocenes
• Ulery, H. E. and Richards, J. H. (1964) The Acid-Catalyzed Cyclization of Acyclic Dienes; Journal of the American Chemical Society; Vol. 86; No. 15; 3113-3117; 10.1021/ja01069a028
• Levenberg, Milton I. and Richards, J. H. (1964) An Analysis of the Nuclear Magnetic Resonance Spectra of Substituted Ferrocenes; Journal of the American Chemical Society; Vol. 86; No. 13; 2634-2637; 10.1021/ja01067a023
• Richards, J. H. and Walker, S. (1964) Mesomeric and electromeric factors in the mononitronaphthylamines; Tetrahedron; Vol. 20; No. 4; 841-853; 10.1016/S0040-4020(01)98416-9
• Fisch, M. H. and Richards, J. H. (1963) The Mechanism of the Photoconversion of Santonin; Journal of the American Chemical Society; Vol. 85; No. 19; 3029-3030; 10.1021/ja00902a038
• Beach, William F. and Richards, John H. (1963) The Structure and Biosynthesis of Nidulin; Journal of Organic Chemistry; Vol. 28; No. 10; 2746-2751; 10.1021/jo01045a061
• Hall, David W. and Richards, John H. (1963) The Acetylation of Some Substituted Ferrocenes; Journal of Organic Chemistry; Vol. 28; No. 6; 1547-1554; 10.1021/jo01041a026
• Richards, John H. (1963) Role of Acetate in Biosynthesis; Antimicrobial Agents and Chemotherapy; Vol. 161; 349-351
• Mock, William and Richards, John H. (1962) The Synthesis of Bridged Ferrocene Derivatives with Functional Groups on the β-Carbon of the Bridge; Journal of Organic Chemistry; Vol. 27; No. 11; 4050-4051; 10.1021/jo01058a504
• Hill, E. Alexander and Richards, John H. (1961) Carbonium Ion Stabilization by Metallocene Nuclei. III. Evidence for Metal Participation; Journal of the American Chemical Society; Vol. 83; No. 20; 4216-4221; 10.1021/ja01481a029
• Hill, E. Alexander and Richards, John H. (1961) Carbonium Ion Stabilization by Metallocene Nuclei. II. α-Metallocenylcarbonium Ions; Journal of the American Chemical Society; Vol. 83; No. 18; 3840-3846; 10.1021/ja01479a025
• Beach, W. F. and Richards, J. H. (1961) The Nature of the Alkyl Groups in Nidulin; Journal of Organic Chemistry; Vol. 26; No. 8; 3011-3012; 10.1021/jo01066a622
• Beach, W. F. and Richards, J. H. (1961) The Structure of Nidulin; Journal of Organic Chemistry; Vol. 26; No. 4; 1339-1340; 10.1021/jo01063a073
• Richards, John H. and Beach, William F. (1961) Long Range Splittings in the NMR Spectra of Isomeric 2-Bromo-2-butenes; Journal of Organic Chemistry; Vol. 26; No. 2; 623-624; 10.1021/jo01061a624
• Carter, R. E. and Richards, J. H. (1961) The biogenesis of phenazine pigments; Journal of the American Chemical Society; Vol. 83; No. 2; 495-496; 10.1021/ja01463a063
• Fraenkel, Gideon and Carter, Robert E., et el. (1960) Chemical Shifts in C_5H_5^-, C_6H_6 and C_7H_7^+; Chemical Shifts and π-Electron Densities; Journal of the American Chemical Society; Vol. 82; No. 22; 5846-5850; 10.1021/ja01507a020
• Ferretti, L. D. and Richards, J. H. (1960) The biogenesis of the mold tropolones; Proceedings of the National Academy of Sciences of the United States of America; Vol. 46; No. 11; 1438-1444; 10.1073/pnas.46.11.1438
• Curphey, T. J. and Santer, J. O., et el. (1960) Protonation of metallocenes by strong acids. Structure of the cation; Journal of the American Chemical Society; Vol. 82; No. 19; 5249-5250; 10.1021/ja01504a062
• Richards, John H. and Ferretti, Louis D. (1960) Tropolone biogenesis; Biochemical and Biophysical Research Communications; Vol. 2; No. 2; 107-110; 10.1016/0006-291X(60)90197-2
• Richards, John H. and Hill, E. Alexander (1959) α-metallocenyl carbonium ions; Journal of the American Chemical Society; Vol. 81; No. 13; 3484-3485; 10.1021/ja01522a089
• Dauben, William G. and Ban, Yoshio, et el. (1957) The Biosynthesis of the Triterpene, Eburicoic Acid: The Utilization of Methyl-labeled Acetate; Journal of the American Chemical Society; Vol. 79; No. 4; 968-970; 10.1021/ja01561a052
• Dauben, William G. and Richards, John H. (1956) The Biosynthesis of the Triterpene, Eburicoic Acid; Journal of the American Chemical Society; Vol. 78; No. 20; 5329-5335; 10.1021/ja01601a047
• Dauben, William G. and Richards, John H. (1955) The Biogenesis of the Triterpene Eburicoic Acid; Chemistry and Industry; Vol. 1955; 94-95