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Volumn 37, Issue 51, 1996, Pages 9233-9236

Transition-metals facilitated electron transfer of semisynthetic myoglobin bearing bis(iminodiacetic acid) moiety

Author keywords

[No Author keywords available]

Indexed keywords

ASCORBIC ACID; METAL ION; MYOGLOBIN;

EID: 0030590960     PISSN: 00404039     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0040-4039(96)02192-2     Document Type: Article
Times cited : (5)

References (12)
  • 3
    • 0012002886 scopus 로고    scopus 로고
    • note
    • 3. BOP: Benzotriazole-1-yl-oxy-tris(dimethylamino) phosphonium hexafluorophosphate DIEA: Diisopropyl ethylamine
  • 4
    • 0011920365 scopus 로고    scopus 로고
    • note
    • 2O: C, 56.64, H, 5.46, N, 11.49%
  • 5
    • 49749199032 scopus 로고
    • 5. F. W. J. Teale, Biochim. Biophys. Acta, 1959, 35, 543.; T. Asakura, "Methods in Enzymology," ed. by S. Fliser and L. Packer, Academic Press, New York, 1978. Part C, p. 446; I. Hamachi, K. Nakamura, A. Fujita and T. Kunitake, J. Am. Chem. Soc., 1993, 115, 4966.
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 543
    • Teale, F.W.J.1
  • 6
    • 0004189217 scopus 로고
    • ed. by S. Fliser and L. Packer, Academic Press, New York
    • 5. F. W. J. Teale, Biochim. Biophys. Acta, 1959, 35, 543.; T. Asakura, "Methods in Enzymology," ed. by S. Fliser and L. Packer, Academic Press, New York, 1978. Part C, p. 446; I. Hamachi, K. Nakamura, A. Fujita and T. Kunitake, J. Am. Chem. Soc., 1993, 115, 4966.
    • (1978) Methods in Enzymology , Issue.PART C , pp. 446
    • Asakura, T.1
  • 7
    • 0000562011 scopus 로고
    • 5. F. W. J. Teale, Biochim. Biophys. Acta, 1959, 35, 543.; T. Asakura, "Methods in Enzymology," ed. by S. Fliser and L. Packer, Academic Press, New York, 1978. Part C, p. 446; I. Hamachi, K. Nakamura, A. Fujita and T. Kunitake, J. Am. Chem. Soc., 1993, 115, 4966.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4966
    • Hamachi, I.1    Nakamura, K.2    Fujita, A.3    Kunitake, T.4
  • 8
    • 0011920230 scopus 로고    scopus 로고
    • note
    • 2-Mb are 413, 542 and 579 nm. These values are identical to those for the corresponding forms of native Mb.
  • 10
    • 0011951528 scopus 로고    scopus 로고
    • note
    • 2+, whereas the α-helix region (two negative peaks at 220 and 208 nm and a positive peak at 190 nm) scarcely changes. Such a transition-metal effect was not observed for the reconstituted Mb with heme 5.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.