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Volumn 305, Issue 4, 2003, Pages 840-845

House fly cytochrome b5 exhibits kinetically trapped hemin and selectivity in hemin binding

Author keywords

Cytochrome b5; Endoplasmic reticulum; Heme; House fly; Mitochondria; Thermal stability

Indexed keywords

APOPROTEIN; CYTOCHROME B5; HEMIN;

EID: 0038581178     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00842-8     Document Type: Article
Times cited : (8)

References (36)
  • 1
    • 0038643798 scopus 로고
    • 5 and the dihydrocoenzyme I-oxidase system in the cecropia silkworm
    • 5 and the dihydrocoenzyme I-oxidase system in the cecropia silkworm. J. Biol. Chem. 209:1954;915-929.
    • (1954) J. Biol. Chem. , vol.209 , pp. 915-929
    • Pappenheimer A.M., Jr.1    Williams, C.M.2
  • 2
    • 0000280194 scopus 로고
    • The isolation and properties of microsomal cytochrome
    • Strittmatter P., Velick S.F. The isolation and properties of microsomal cytochrome. J. Biol. Chem. 221:1956;253-264.
    • (1956) J. Biol. Chem. , vol.221 , pp. 253-264
    • Strittmatter, P.1    Velick, S.F.2
  • 3
    • 0015057049 scopus 로고
    • 5 that contains an additional hydrophobic sequence of 40 amino acid residues
    • 5 that contains an additional hydrophobic sequence of 40 amino acid residues. Proc. Natl. Acad. Sci. USA. 68:1971;1042-1046.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 1042-1046
    • Spatz, L.1    Strittmatter, P.2
  • 4
    • 0024402568 scopus 로고
    • 5 and its topology in the microsomal membrane
    • 5 and its topology in the microsomal membrane. Biochim. Biophys. Acta. 997:1989;121-130.
    • (1989) Biochim. Biophys. Acta , vol.997 , pp. 121-130
    • Ozols, J.1
  • 9
    • 0015897918 scopus 로고
    • 5-like hemoprotein associated with outer mitochondrial membrane of rat liver
    • 5-like hemoprotein associated with outer mitochondrial membrane of rat liver. J. Biochem. 74:1973;161-173.
    • (1973) J. Biochem. , vol.74 , pp. 161-173
    • Fukushima, K.1    Sato, R.2
  • 16
    • 49749199032 scopus 로고
    • Cleavage of the haem-protein link by acid methylethylketone
    • Teale F.W.J. Cleavage of the haem-protein link by acid methylethylketone. Biochim. Biophys. Acta. 35:1959;453.
    • (1959) Biochim. Biophys. Acta , vol.35 , pp. 453
    • Teale, F.W.J.1
  • 20
    • 0027364062 scopus 로고
    • 5 in Escherichia coli and a study of the solution structure and stability of variant proteins
    • 5 in Escherichia coli and a study of the solution structure and stability of variant proteins. Protein Eng. 6:1993;953-964.
    • (1993) Protein Eng. , vol.6 , pp. 953-964
    • Hewson, R.1    Newbold, R.J.2    Whitford, D.3
  • 27
    • 0000380550 scopus 로고
    • Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: Evidence for intramolecular reorientation about a heme two-fold axis
    • LaMar G.N., Toi H., Krishnamoorthi R. Proton NMR investigation of the rate and mechanism of heme rotation in sperm whale myoglobin: evidence for intramolecular reorientation about a heme two-fold axis. J. Am. Chem. Soc. 106:1984;6395-6401.
    • (1984) J. Am. Chem. Soc. , vol.106 , pp. 6395-6401
    • LaMar, G.N.1    Toi, H.2    Krishnamoorthi, R.3
  • 28
    • 0014788195 scopus 로고
    • Aggregation of ferrihaems. Dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solution
    • Brown S.B., Dean T.C., Jones P. Aggregation of ferrihaems. Dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solution. Biochem. J. 117:1970;733-740.
    • (1970) Biochem. J. , vol.117 , pp. 733-740
    • Brown, S.B.1    Dean, T.C.2    Jones, P.3
  • 29
    • 0001062291 scopus 로고
    • Kinetic studies on the reaction between native globin and heme derivatives
    • Gibson Q.H., Antonini E. Kinetic studies on the reaction between native globin and heme derivatives. Biochem. J. 77:1960;328-341.
    • (1960) Biochem. J. , vol.77 , pp. 328-341
    • Gibson, Q.H.1    Antonini, E.2
  • 30
    • 0020533291 scopus 로고
    • The kinetic mechanism of heme binding to human apohemoglobin
    • Rose M.Y., Olson J.S. The kinetic mechanism of heme binding to human apohemoglobin. J. Biol. Chem. 258:1983;4298-4303.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4298-4303
    • Rose, M.Y.1    Olson, J.S.2
  • 31
    • 0029737895 scopus 로고    scopus 로고
    • The association rate constant for heme binding to globin is independent of protein structure
    • Hargrove M.S., Barrick D., Olson J.S. The association rate constant for heme binding to globin is independent of protein structure. Biochemistry. 35:1996;11293-11299.
    • (1996) Biochemistry , vol.35 , pp. 11293-11299
    • Hargrove, M.S.1    Barrick, D.2    Olson, J.S.3
  • 33
    • 0028691707 scopus 로고
    • 5 involvement in cytochrome P450 monooxygenase activities in house fly microsomes
    • 5 involvement in cytochrome P450 monooxygenase activities in house fly microsomes. Arch. Insect Biochem. Physiol. 27:1994;205-216.
    • (1994) Arch. Insect Biochem. Physiol. , vol.27 , pp. 205-216
    • Zhang, M.1    Scott, J.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.