[
    {
        "id": "authors:nx2e2-7cp92",
        "collection": "authors",
        "collection_id": "nx2e2-7cp92",
        "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20180406-080326896",
        "type": "book_section",
        "title": "Donor\u2014Acceptor Electronic Coupling in Ruthenium-Modified Heme Proteins",
        "book_title": "Mechanistic Bioinorganic Chemistry",
        "author": [
            {
                "family_name": "Casimiro",
                "given_name": "Danilo R.",
                "clpid": "Casimiro-D-R"
            },
            {
                "family_name": "Beratan",
                "given_name": "David N.",
                "clpid": "Beratan-D-N"
            },
            {
                "family_name": "Onuchic",
                "given_name": "Jos\u00e9 Nelson",
                "clpid": "Onuchic-J-N"
            },
            {
                "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": "The rates of electron transfer (ET) in six Ru-modified cytochrome c derivatives were analyzed in terms of four theoretical models describing donor-acceptor electronic coupling. The simplest model, which treats the protein as a homogeneous medium, fails to describe the variations in ET rates with changes in donor-acceptor separation. The three other models explicitly account for the inhomogeneity of the polypeptide matrix and are more successful in describing the electronic couplings. Calculations of relative coupling strengths give results within an order of magnitude of experimentally determined values for cytochrome c. The homogeneousmedium model is more successful in describing ET in Ru-modified myoglobin, and two of the inhomogeneous-medium models suggest that multiple pathways are important in mediating the electronic coupling.",
        "doi": "10.1021/ba-1995-0246.ch018",
        "isbn": "9780841230620",
        "publisher": "American Chemical Society",
        "place_of_publication": "Washington, DC",
        "publication_date": "1996-05-05",
        "pages": "471-485"
    },
    {
        "id": "authors:jpyfh-cg421",
        "collection": "authors",
        "collection_id": "jpyfh-cg421",
        "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20150505-090548164",
        "type": "book_section",
        "title": "Long-Range Electron Transfer in Ruthenium-Modified Cytochromes c. \u03c3-Tunneling Pathways through Aromatic Residues",
        "book_title": "Research in Photosynthesis",
        "author": [
            {
                "family_name": "Casimiro",
                "given_name": "Danilo R.",
                "clpid": "Casimiro-D-R"
            },
            {
                "family_name": "Winkler",
                "given_name": "Jay R.",
                "orcid": "0000-0002-4453-9716",
                "clpid": "Winkler-J-R"
            },
            {
                "family_name": "Richards",
                "given_name": "John H.",
                "clpid": "Richards-J-H"
            },
            {
                "family_name": "Gray",
                "given_name": "Harry B.",
                "orcid": "0000-0002-7937-7876",
                "clpid": "Gray-H-B"
            }
        ],
        "contributor": [
            {
                "family_name": "Murata",
                "given_name": "N.",
                "clpid": "Murata-N"
            }
        ],
        "abstract": "Studies of intramolecular electron transfer (ET) in chemically-modified\nmetalloproteins have suggested that the long-range donor-acceptor coupling is\ndetermined by the structure of the bridging polypeptide medium. One issue that\nremains largely unclear is whether aromatic side chains in the intervening medium\nenhance these electronic couplings to a significant extent To address this issue, we\nhave prepared site-directed mutants of Saccharomyces cerevisiae iso-1-cytchrome c,\nwhere in each case a surface histidine for ruthenium labeling is introduced at either\nposition 58 or 66. Based on the crystal structure of the protein, a tryptophan (at\nposition 59) or a tyrosine (67) is found along the ET path between the Ru-modified\nhistidine and the heme. In order to probe the role of the bridging Tyr67 in the His66\nvariant, this internal residue has been replaced with a phenylalanine.",
        "isbn": "9780792320913",
        "publisher": "Kluwer",
        "publication_date": "1992",
        "pages": "829-832"
    }
]