DOI: 10.1111/j.1432-1033.1971.tb01523.x. A Study of the Reduction and Oxidation of Human Ceruloplasmin

A Study of the Reduction and Oxidation of Human Ceruloplasmin

10.1111/j.1432-1033.1971.tb01523.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

The stopped‐flow technique was utilized to measure the 610 and 340 nm absorbances of human ceruloplasmin during oxidation and reduction reactions. The results confirm earlier observations that the chromophores giving rise to these absorbances are different electron acceptors. Under steady state conditions both chromophores were partially reduced which indicates that they participate in the oxidase reaction. Oxidation rates for the 610 and 340 nm chromophores of completely reduced ceruloplasmin were too high to be compatible with the respective steady state absorbances. These results, together with a comparison of the oxidation rates for Type 1 copper of partially and completely reduced protein, showed that the oxidation rate for one chromophore is influenced by the oxidation states of the other and/or the nonchromophoric paramagnetic copper (Type 2). Therefore, the oxidase mechanism appears to involve concerted transfer of electrons from the 610 and 340 nm chromophores and possibly Type 2 copper.

Bibliography

Carrico, R. J., MalmstrÃ¼m, B. G., & VÃ¤nngÃ¥rd, T. (1971). A Study of the Reduction and Oxidation of Human Ceruloplasmin. European Journal of Biochemistry, 22(1), 127â133. Portico.

Authors 3

Robert J. Carrico (first)
Bo G. Malmstrüm (additional)
Tore Vänngård (additional)

References 23 Referenced 49

10.1016/0005-2744(68)90001-6
10.1002/9780470122785.ch4
10.1016/S0022-2836(62)80035-7
10.1016/S0022-2836(67)80005-6
10.1111/j.1432-1033.1971.tb01422.x
10.1016/0005-2795(70)90168-6
10.1016/B978-1-4832-1333-0.50033-1
10.1016/0006-3002(63)90624-3
10.1016/S0021-9258(18)99620-1
10.1016/0003-9861(67)90103-8
10.1016/0304-4165(68)90105-0
10.1111/j.1432-1033.1969.tb19600.x
10.1016/0005-2728(68)90175-8
10.1016/0003-2697(67)90038-3
{'key': 'e_1_2_1_16_2', 'first-page': '537', 'volume-title': 'Colorimetric Metal Analysis', 'author': 'Sandell E. B.', 'year': '1959'} / Colorimetric Metal Analysis by Sandell E. B. (1959)
{'key': 'e_1_2_1_17_2', 'volume-title': 'Oxidases and Related Redox Systems II', 'author': 'Andréasson L.‐E.'} / Oxidases and Related Redox Systems II by Andréasson L.‐E.
10.1016/S0021-9258(18)99669-9
10.1016/S0021-9258(17)36402-5
10.1042/bj1030289
10.1085/jgp.49.1.213
10.1016/S0021-9258(18)97760-4
10.1111/j.1432-1033.1969.tb00620.x
10.1016/0005-2728(70)90060-5

Dates

Type	When
Created	20 years, 6 months ago (March 3, 2005, 9:21 a.m.)
Deposited	1 year, 9 months ago (Nov. 23, 2023, 9:16 a.m.)
Indexed	1 year, 7 months ago (Jan. 18, 2024, 4:11 a.m.)
Issued	54 years ago (Sept. 1, 1971)
Published	54 years ago (Sept. 1, 1971)
Published Online	20 years, 6 months ago (March 3, 2005)
Published Print	54 years ago (Sept. 1, 1971)

Funders 0

None

BibTeX

@article{Carrico_1971, title={A Study of the Reduction and Oxidation of Human Ceruloplasmin: Evidence that a Diamagnetic Chromophore in the Enzyme Participates in the Oxidase Mechanism}, volume={22}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1971.tb01523.x}, DOI={10.1111/j.1432-1033.1971.tb01523.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={Carrico, Robert J. and Malmstrüm, Bo G. and Vänngård, Tore}, year={1971}, month=sep, pages={127–133} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2024,
        1,
        18
      ]
    ],
    "date-time": "2024-01-18T09:11:42Z",
    "timestamp": 1705569102890
  },
  "reference-count": 23,
  "publisher": "Wiley",
  "issue": "1",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2005,
            3,
            3
          ]
        ],
        "date-time": "2005-03-03T00:00:00Z",
        "timestamp": 1109808000000
      },
      "content-version": "vor",
      "delay-in-days": 12237,
      "URL": "http://onlinelibrary.wiley.com/termsAndConditions#vor"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        1971,
        9
      ]
    ]
  },
  "abstract": "<jats:p>The stopped\u2010flow technique was utilized to measure the 610 and 340 nm absorbances of human ceruloplasmin during oxidation and reduction reactions. The results confirm earlier observations that the chromophores giving rise to these absorbances are different electron acceptors. Under steady state conditions both chromophores were partially reduced which indicates that they participate in the oxidase reaction. Oxidation rates for the 610 and 340 nm chromophores of completely reduced ceruloplasmin were too high to be compatible with the respective steady state absorbances. These results, together with a comparison of the oxidation rates for Type 1 copper of partially and completely reduced protein, showed that the oxidation rate for one chromophore is influenced by the oxidation states of the other and/or the nonchromophoric paramagnetic copper (Type 2). Therefore, the oxidase mechanism appears to involve concerted transfer of electrons from the 610 and 340 nm chromophores and possibly Type 2 copper.</jats:p>",
  "DOI": "10.1111/j.1432-1033.1971.tb01523.x",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2005,
        3,
        3
      ]
    ],
    "date-time": "2005-03-03T14:21:26Z",
    "timestamp": 1109859686000
  },
  "page": "127-133",
  "source": "Crossref",
  "is-referenced-by-count": 49,
  "title": "A Study of the Reduction and Oxidation of Human Ceruloplasmin",
  "prefix": "10.1111",
  "volume": "22",
  "author": [
    {
      "given": "Robert J.",
      "family": "Carrico",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Bo G.",
      "family": "Malmstr\u00fcm",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Tore",
      "family": "V\u00e4nng\u00e5rd",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "311",
  "published-online": {
    "date-parts": [
      [
        2005,
        3,
        3
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_2_1_2_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0005-2744(68)90001-6"
    },
    {
      "key": "e_1_2_1_3_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/9780470122785.ch4"
    },
    {
      "key": "e_1_2_1_4_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0022-2836(62)80035-7"
    },
    {
      "key": "e_1_2_1_5_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0022-2836(67)80005-6"
    },
    {
      "key": "e_1_2_1_6_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1971.tb01422.x"
    },
    {
      "key": "e_1_2_1_7_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0005-2795(70)90168-6"
    },
    {
      "key": "e_1_2_1_8_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/B978-1-4832-1333-0.50033-1"
    },
    {
      "key": "e_1_2_1_9_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0006-3002(63)90624-3"
    },
    {
      "key": "e_1_2_1_10_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(18)99620-1"
    },
    {
      "key": "e_1_2_1_11_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0003-9861(67)90103-8"
    },
    {
      "key": "e_1_2_1_12_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0304-4165(68)90105-0"
    },
    {
      "key": "e_1_2_1_13_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1969.tb19600.x"
    },
    {
      "key": "e_1_2_1_14_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0005-2728(68)90175-8"
    },
    {
      "key": "e_1_2_1_15_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0003-2697(67)90038-3"
    },
    {
      "key": "e_1_2_1_16_2",
      "first-page": "537",
      "volume-title": "Colorimetric Metal Analysis",
      "author": "Sandell E. B.",
      "year": "1959"
    },
    {
      "key": "e_1_2_1_17_2",
      "volume-title": "Oxidases and Related Redox Systems II",
      "author": "Andr\u00e9asson L.\u2010E."
    },
    {
      "key": "e_1_2_1_18_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(18)99669-9"
    },
    {
      "key": "e_1_2_1_19_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(17)36402-5"
    },
    {
      "key": "e_1_2_1_20_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1042/bj1030289"
    },
    {
      "key": "e_1_2_1_21_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1085/jgp.49.1.213"
    },
    {
      "key": "e_1_2_1_22_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(18)97760-4"
    },
    {
      "key": "e_1_2_1_23_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1969.tb00620.x"
    },
    {
      "key": "e_1_2_1_24_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0005-2728(70)90060-5"
    }
  ],
  "container-title": "European Journal of Biochemistry",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1432-1033.1971.tb01523.x",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://febs.onlinelibrary.wiley.com/doi/pdf/10.1111/j.1432-1033.1971.tb01523.x",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        11,
        23
      ]
    ],
    "date-time": "2023-11-23T14:16:44Z",
    "timestamp": 1700749004000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1971.tb01523.x"
    }
  },
  "subtitle": [
    "Evidence that a Diamagnetic Chromophore in the Enzyme Participates in the Oxidase Mechanism"
  ],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1971,
        9
      ]
    ]
  },
  "references-count": 23,
  "journal-issue": {
    "issue": "1",
    "published-print": {
      "date-parts": [
        [
          1971,
          9
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1111/j.1432-1033.1971.tb01523.x"
  ],
  "URL": "http://dx.doi.org/10.1111/j.1432-1033.1971.tb01523.x",
  "relation": {},
  "ISSN": [
    "0014-2956",
    "1432-1033"
  ],
  "subject": [],
  "container-title-short": "European Journal of Biochemistry",
  "published": {
    "date-parts": [
      [
        1971,
        9
      ]
    ]
  }
}