[ { "id": "authors:n2xtx-8db64", "collection": "authors", "collection_id": "n2xtx-8db64", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20171107-082821022", "type": "article", "title": "The Human Genome Project", "author": [ { "family_name": "Yager", "given_name": "Thomas D.", "clpid": "Yager-T-D" }, { "family_name": "Zewert", "given_name": "Thomas E.", "clpid": "Zewert-T-E" }, { "family_name": "Hood", "given_name": "Leroy E.", "orcid": "0000-0001-7158-3678", "clpid": "Hood-L-E" } ], "abstract": "The Human Genome Project (HGP) is a coordinated\nworldwide effort to precisely map the human genome\nand the genomes of selected model organisms. The\nfirst explicit proposal for this project dates from 1985\nalthough its foundations (both conceptual and technological)\ncan be traced back many years in genetics, molecular biology, and biotechnology The HGP has matured rapidly and is producing results of great significance.", "doi": "10.1021/ar00040a002", "issn": "0001-4842", "publisher": "American Chemical Society", "publication": "Accounts of Chemical Research", "publication_date": "1994-04-01", "series_number": "4", "volume": "27", "issue": "4", "pages": "94-100" }, { "id": "authors:7br4x-m2p96", "collection": "authors", "collection_id": "7br4x-m2p96", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180529-152346680", "type": "article", "title": "Environment of the Heme in Myoglobins. NMRD and EPR Spectroscopy of Val68X (X = Asn, Asp, and Glu) Mutants of Human Myoglobin", "author": [ { "family_name": "Zewert", "given_name": "Thomas E.", "clpid": "Zewert-T-E" }, { "family_name": "Gray", "given_name": "Harry B.", "orcid": "0000-0002-7937-7876", "clpid": "Gray-H-B" }, { "family_name": "Bertini", "given_name": "Ivano", "clpid": "Bertini-I" } ], "abstract": "Analyses of the temperature dependences and shapes of nuclear magnetic relaxation dispersion (NMRD) signals of site-directed mutants of human myoglobin indicate that a water molecule is bound to the sixth coordination site of the ferric heme in proteins in which the valine at position 68 is changed to either aspartate (Val68Asp) or asparagine (Val68Asn). Both NMRD data and electron paramagetic resonance (EPR) spectra show that carboxylate is axially ligated to Fe(III) in the Va168Glu mutant. The EPR spectra of the Va168Asp and Va168Asn derivatives show much smaller rhombic splittings than the spectrum of the Va168Glu protein.", "doi": "10.1021/ja00083a001", "issn": "0002-7863", "publisher": "American Chemical Society", "publication": "Journal of the American Chemical Society", "publication_date": "1994-02-23", "series_number": "4", "volume": "116", "issue": "4", "pages": "1169-1173" }, { "id": "authors:1801f-ge366", "collection": "authors", "collection_id": "1801f-ge366", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20150430-135323908", "type": "article", "title": "Electron Transfer in Ruthenium/Zinc Porphyrin Derivatives of\n Recombinant Human Myoglobins. Analysis of Tunneling Pathways in Myoglobin and Cytochrome c", "author": [ { "family_name": "Casimiro", "given_name": "Danilo R.", "clpid": "Casimiro-D-R" }, { "family_name": "Wong", "given_name": "Luet-L.", "clpid": "Wong-Luet-Lok" }, { "family_name": "Col\u00f3n", "given_name": "Jorge L.", "clpid": "Col\u00f3n-J-L" }, { "family_name": "Zewert", "given_name": "Thomas E.", "clpid": "Zewert-T-E" }, { "family_name": "Richards", "given_name": "John H.", "clpid": "Richards-J-H" }, { "family_name": "Chang", "given_name": "I-Jy", "clpid": "Chang-I-Jy" }, { "family_name": "Winkler", "given_name": "Jay R.", "orcid": "0000-0002-4453-9716", "clpid": "Winkler-J-R" }, { "family_name": "Gray", "given_name": "Harry B.", "orcid": "0000-0002-7937-7876", "clpid": "Gray-H-B" } ], "abstract": "Site-directed mutants of human myoglobin have been prepared and characterized; each protein has a single\nsurface-modifiable histidine (at position 48, 70, or 83). The proteins were modified by covalent attachment of pentaammineruthenium (a_5Ru) to the surface histidine and substitution of zinc mesoporphyrin IX diacid (ZnP) for the heme. Donor-acceptor separations (edge-edge distances d) in the modified proteins are 9.5 \u00c5, His70; 12.7 \u00c5, His48; and 15.5 \u00c5, His83. Rates of photoinduced electron transfer in these ruthenium-modified myoglobins were measured by transient absorption spectroscopy. The ^(3)ZnP* \u2192 Ru^3+ rate constants are 1.6 \u00d7 10^7 (His70), 7.2 \u00d7 10^4 (His48), and 4.0 \u00d7 10^2 s^-1 (His83) (-\u0394G\u00b0= 0.82 eV); charge-recombination (Ru^2+ \u2192 ZnP^+) rates are 1.1 \u00d7 10^5 (His48) and 7.3 \u00d7 10^2 s^-1 (His83) (-\u0394G\u00b0 = 0.96 eV). Activationless (maximum) rates assuming h = 1.3 eV are 7.2 X lo7 (His70), 3.3 \u00d7 10^5 (His48) and 1.8 \u00d7 10^3 s^-1 (His83). Distant electronic couplings, which limit the maximum rates in the modified myoglobins, have been analyzed along with data from Ru-modified cytochromes c in terms of a tunneling pathway model. Single dominant pathways adequately describe the electronic couplings in cytochrome c but do not satisfactorily account for the myoglobin couplings. The correlation of electronic coupling with tunneling length for myoglobin is improved significantly by the inclusion of multiple pathways.", "doi": "10.1021/ja00057a037", "issn": "0002-7863", "publisher": "American Chemical Society", "publication": "Journal of the American Chemical Society", "publication_date": "1993-02-24", "series_number": "4", "volume": "115", "issue": "4", "pages": "1485-1489" }, { "id": "authors:0wkpb-60z65", "collection": "authors", "collection_id": "0wkpb-60z65", "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20150128-121300760", "type": "article", "title": "Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobin", "author": [ { "family_name": "Varadarajan", "given_name": "Raghavan", "clpid": "Varadarajan-R" }, { "family_name": "Zewert", "given_name": "Thomas E.", "clpid": "Zewert-T-E" }, { "family_name": "Gray", "given_name": "Harry B.", "orcid": "0000-0002-7937-7876", "clpid": "Gray-H-B" }, { "family_name": "Boxer", "given_name": "Steven G.", "clpid": "Boxer-S-G" } ], "abstract": "The temperature dependences of the reduction potentials (E\u00b0') of wild-type human myoglobin (Mb) and three site-directed mutants have been measured by the use of thin-layer spectroelectrochemistry. Residue Val68, which is in van der Waals contact with the heme in Mb, has been replaced by Glu, Asp, and Asn. The changes in E degrees' and the standard entropy (\u0394S\u00b0') and enthalpy (\u0394H\u00b0') of reduction in the mutant proteins were determined relative to values for wild type; the change in E\u00b0' at 25 \u00b0C was about -200 millivolts for the Glu and Asp mutants, and about -80 millivolts for the Asn mutant. At pH 7.0, reduction of Fe(III) to Fe(II) in the Glu and Asp mutants is accompanied by uptake of a proton by the protein. These studies demonstrate that Mb can tolerate substitution of a buried hydrophobic group by potentially charged and polar residues and that such amino acid replacements can lead to substantial changes in the redox thermodynamics of the protein.", "doi": "10.1126/science.2563171", "issn": "0036-8075", "publisher": "American Association for the Advancement of Science", "publication": "Science", "publication_date": "1989-01-06", "series_number": "4887", "volume": "243", "issue": "4887", "pages": "69-72" } ]