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Volumn 351, Issue 3, 2000, Pages 595-605

The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: An EPR study

Author keywords

Hemichromes; Histidine; Human blood; Mechanism simulation

Indexed keywords

HEME; HEMOGLOBIN CHAIN; HISTIDINE; METHEMOGLOBIN; METMYOGLOBIN;

EID: 0034331816     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3510595     Document Type: Article
Times cited : (48)

References (39)
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  • 2
    • 0007452063 scopus 로고
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    • (1971) , vol.21
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  • 6
    • 0000382264 scopus 로고
    • A unified theory for low spin forms of all ferric heine proteins as studied by EPR
    • Probes of Structure and Function of Macromolecules and Membranes, (Chance, B., Yonetani, T. and Mildvan, A. S., eds.), Academic Press, New York
    • (1971) , vol.2 , pp. 215-229
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  • 32
    • 0000717649 scopus 로고
    • Effect of low temperature on the absorption spectra of haemoproteins; with observations on the absorption spectrum of oxygen
    • (1949) Nature (London) , vol.164 , pp. 254-259
    • Keilin, D.1    Hartree, E.F.2
  • 39
    • 0007378480 scopus 로고
    • The iron atom displacement in deoxyhemoglobin: A spin-state or nonbonded repulsion effect?
    • Frontiers of Biological Energetics (Dutton, P. L., Leigh, J. S. Scarpa, A. eds.), Academic Press, Inc, New York
    • (1978) , vol.2 , pp. 1017-1023
    • Scheidt, W.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.