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Volumn 126, Issue 21, 2004, Pages 6579-6589

Ferrous binding to the multicopper oxidases Saccharomyces cerevisiae Fet3p and human ceruloplasmin: Contributions to ferroxidase activity

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ELECTRONIC STRUCTURE; ENERGY TRANSFER; MUTAGENESIS; OXIDATION; SUBSTRATES;

EID: 2542515319     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja049220t     Document Type: Article
Times cited : (61)

References (94)
  • 32
  • 41
    • 0036399802 scopus 로고    scopus 로고
    • Valentine, J. S., Gralla, E. B., Eds.; Academic Press Inc: London, UK
    • Kosman, D. J. In Copper-Containing Proteins; Valentine, J. S., Gralla, E. B., Eds.; Academic Press Inc: London, UK, 2002; Vol. 60, pp 221-269.
    • (2002) Copper-Containing Proteins , vol.60 , pp. 221-269
    • Kosman, D.J.1
  • 77
    • 2542594195 scopus 로고    scopus 로고
    • note
    • The slopes for the Y354 mutants data differ from those of WT and E185 mutants by about 20 mV. This could reflect reduction of the T1 site in these proteins being a > 1 electron process, which is plausible given the presence of other Cu sites in the protein (trinuclear cluster) with redox potentials comparable to that of the T1 Cu site. Alternatively, it can also reflect some protein denaturation during the experiment, which was observed in the Y354 mutants case.
  • 86
    • 2542554515 scopus 로고    scopus 로고
    • note
    • The standard reduction potential for the Fe(II)/Fe(III) couple in aqueous solution is +770 mV. The redox potential at pH 6.5 was calculated using the stability constants for the relevant iron hydroxide complexes at this pH range, taken from the Pourvaix diagrams.
  • 87
    • 2542638169 scopus 로고    scopus 로고
    • note
    • II, respectively.
  • 93
    • 2542623165 scopus 로고    scopus 로고
    • note
    • This trend refers to the rate constant for the fast phase.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.