[
    {
        "id": "authors:y75ar-33v07",
        "collection": "authors",
        "collection_id": "y75ar-33v07",
        "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20110603-135022605",
        "type": "book_section",
        "title": "Overexpression and Purification of the Particulate Methane Monooxygenase from Methylococcus capsulatus (Bath)",
        "book_title": "Methods in Methane Metabolism. Part B, Methanotrophy",
        "author": [
            {
                "family_name": "Chan",
                "given_name": "Sunney I.",
                "orcid": "0000-0002-5348-2723",
                "clpid": "Chan-S-I"
            },
            {
                "family_name": "Nguyen",
                "given_name": "H.-Hoa T.",
                "clpid": "Nguyen-Hiep-Hoa-T"
            },
            {
                "family_name": "Chen",
                "given_name": "Kelvin H.-C.",
                "clpid": "Chen-Kelvin-H-C"
            },
            {
                "family_name": "Yu",
                "given_name": "Steve S.-F.",
                "orcid": "0000-0002-3462-065X",
                "clpid": "Yu-Steve-S-F"
            }
        ],
        "contributor": [
            {
                "family_name": "Rosenzweig",
                "given_name": "Amy C.",
                "clpid": "Rosenzweig-A-C"
            },
            {
                "family_name": "Ragsdale",
                "given_name": "Stephen W.",
                "clpid": "Ragsdale-S-W"
            }
        ],
        "abstract": "The particulate methane monooxygenase (pMMO) is a multi-copper enzyme that mediates the facile conversion of methane to methanol in methanotrophic bacteria. As a membrane-bound multi-subunit metalloprotein, the highly active protein has been difficult to isolate and purify to homogeneity for biochemical and biophysical studies. In this chapter, we describe a method to overexpress pMMO with good specific activity in high yields in the intracytoplasmic membranes of the host organism, together with two protocols to isolate and purify the enzyme from pMMO-enriched membranes without loss of the copper cofactors and enzymatic activity.",
        "doi": "10.1016/B978-0-12-386905-0.00012-7",
        "isbn": "9780123869050",
        "publisher": "Elsevier",
        "place_of_publication": "Amsterdam",
        "publication_date": "2011",
        "pages": "177-193"
    },
    {
        "id": "authors:ry7ry-1nw89",
        "collection": "authors",
        "collection_id": "ry7ry-1nw89",
        "cite_using_url": "https://resolver.caltech.edu/CaltechAUTHORS:20200512-123507275",
        "type": "book_section",
        "title": "Rapid Formation of a Semiquinone Species on Oxidation of Quinol by the Cytochrome bo 3 Oxidase from Escherichia coli",
        "book_title": "Oxygen Homeostasis and Its Dynamics",
        "author": [
            {
                "family_name": "Osborne",
                "given_name": "Jeffrey P.",
                "clpid": "Osborne-J-P"
            },
            {
                "family_name": "Musser",
                "given_name": "Sigfried M.",
                "clpid": "Musser-S-M"
            },
            {
                "family_name": "Schultz",
                "given_name": "Brian E.",
                "clpid": "Schultz-B-E"
            },
            {
                "family_name": "Edmondson",
                "given_name": "Dale E.",
                "clpid": "Edmondson-D-E"
            },
            {
                "family_name": "Chan",
                "given_name": "Sunney I.",
                "orcid": "0000-0002-5348-2723",
                "clpid": "Chan-S-I"
            },
            {
                "family_name": "Gennis",
                "given_name": "Robert B.",
                "clpid": "Gennis-R-B"
            }
        ],
        "contributor": [
            {
                "family_name": "Ishimura",
                "given_name": "Yuzuru",
                "clpid": "Ishimura-Yuzuru"
            },
            {
                "family_name": "Shimada",
                "given_name": "Hideo",
                "clpid": "Shimada-Hideo"
            },
            {
                "family_name": "Suematsu",
                "given_name": "Makoto",
                "clpid": "Suematsu-Makoto"
            }
        ],
        "abstract": "Many bacterial oxidases utilize dihydroquinols, such as ubiquinol or menaquinol, rather than cytochrome c as a substrate. The best-characterized ubiquinol oxidase is cytochrome bo \u2083 from Escherichia coli. In this work, the initial oxidation of ubiquinol by this ubiquinol oxidase is examined. Stopped-flow UV-visible spectroscopy and rapid freeze-quench electron paramagnetic resonance (EPR) spectroscopies were used to examine the oxidation of ubiquinol-2 (UQ\u2082H\u2082) by cytochrome bo \u2083 under multiple turnover conditions. The results show the rapid appearance of the semiquinone radical, coincident with the reduction of the low-spin heme b component of the enzyme. The rate of formation of the semiquinone radical is consistent with the proposition that this is a kinetically relevant intermediate in the reaction sequence. As UQ\u2082H\u2082 is depleted, the radical decays and the enzyme forms a \"peroxy,\" or P, complex with dioxygen. No detectable protein radical is associated with the P complex.",
        "doi": "10.1007/978-4-431-68476-3_4",
        "isbn": "978-4-431-68478-7",
        "publisher": "Springer",
        "place_of_publication": "Tokyo",
        "publication_date": "1998",
        "pages": "33-39"
    }
]