메뉴 건너뛰기




Volumn 84, Issue 1, 2010, Pages 125-128

Nitric oxide inhibits the formation of zinc protoporphyrin IX and protoporphyrin IX

Author keywords

Nitric oxide; Nitrite; Parma ham; Protoporphyrin IX; Zinc protoporphyrin IX

Indexed keywords

CHELATING AGENT; FOOD PRESERVATIVE; NITRIC OXIDE; NITRIC OXIDE DONOR; PROTOPORPHYRIN; PROTOPORPHYRIN ZINC; SODIUM NITRITE;

EID: 70349733408     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2009.08.036     Document Type: Article
Times cited : (24)

References (24)
  • 1
    • 30844449016 scopus 로고    scopus 로고
    • Zn-porphyrin formation in cured meat products: Effect of added salt and nitrite
    • Adamsen C.E., Møller J.K.S., Laursen K., Olsen K., and Skibsted L.H. Zn-porphyrin formation in cured meat products: Effect of added salt and nitrite. Meat Science 72 (2006) 672-679
    • (2006) Meat Science , vol.72 , pp. 672-679
    • Adamsen, C.E.1    Møller, J.K.S.2    Laursen, K.3    Olsen, K.4    Skibsted, L.H.5
  • 4
    • 0028047783 scopus 로고
    • Human ferrochelatase is an iron-sulfur protein
    • Dailey H.A., Finnegan M.G., and Johnson M.K. Human ferrochelatase is an iron-sulfur protein. Biochemistry 33 (1994) 403-407
    • (1994) Biochemistry , vol.33 , pp. 403-407
    • Dailey, H.A.1    Finnegan, M.G.2    Johnson, M.K.3
  • 5
    • 0029023937 scopus 로고
    • Nitric oxide-mediated inactivation of mammalian ferrochelatase in-vivo and in-vitro - possible involvement of the iron-sulfur cluster of the enzyme
    • Furukawa T., Kohno H., Tokunaga R., and Taketani S. Nitric oxide-mediated inactivation of mammalian ferrochelatase in-vivo and in-vitro - possible involvement of the iron-sulfur cluster of the enzyme. Biochemical Journal 310 (1995) 533-538
    • (1995) Biochemical Journal , vol.310 , pp. 533-538
    • Furukawa, T.1    Kohno, H.2    Tokunaga, R.3    Taketani, S.4
  • 6
    • 0017146561 scopus 로고
    • Nitrate, fumarate, and oxygen as electron acceptors for a late step in microbial heme synthesis
    • Jacobs N.J., and Jacobs J.M. Nitrate, fumarate, and oxygen as electron acceptors for a late step in microbial heme synthesis. Biochimica et Biophysica Acta 449 (1976) 1-9
    • (1976) Biochimica et Biophysica Acta , vol.449 , pp. 1-9
    • Jacobs, N.J.1    Jacobs, J.M.2
  • 7
    • 0022399476 scopus 로고
    • Oxidation of protoporphyrinogen in the obligate anaerobe Desulfovibrio gigas
    • Klemm D.J., and Barton L.L. Oxidation of protoporphyrinogen in the obligate anaerobe Desulfovibrio gigas. Journal of Bacteriology 164 (1985) 316-320
    • (1985) Journal of Bacteriology , vol.164 , pp. 316-320
    • Klemm, D.J.1    Barton, L.L.2
  • 13
    • 0032710987 scopus 로고    scopus 로고
    • Zinc protoporphyrin: A metabolite with a mission
    • Labbe R.F., Vreman H.J., and Stevenson D.K. Zinc protoporphyrin: A metabolite with a mission. Clinical Chemistry 45 (1999) 2060-2072
    • (1999) Clinical Chemistry , vol.45 , pp. 2060-2072
    • Labbe, R.F.1    Vreman, H.J.2    Stevenson, D.K.3
  • 14
    • 36749061359 scopus 로고    scopus 로고
    • Quantification of zinc-porphyrin in dry-cured ham products by spectroscopic methods: Comparison of absorption, fluorescence and X-ray fluorescence spectroscopy
    • Laursen K., Adamsen C.E., Laursen J., Olsen K., and Møller J.K.S. Quantification of zinc-porphyrin in dry-cured ham products by spectroscopic methods: Comparison of absorption, fluorescence and X-ray fluorescence spectroscopy. Meat Science 78 (2008) 336-341
    • (2008) Meat Science , vol.78 , pp. 336-341
    • Laursen, K.1    Adamsen, C.E.2    Laursen, J.3    Olsen, K.4    Møller, J.K.S.5
  • 15
    • 0016671103 scopus 로고
    • The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae
    • Poulson R., and Polglase W.J. The enzymic conversion of protoporphyrinogen IX to protoporphyrin IX. Protoporphyrinogen oxidase activity in mitochondrial extracts of Saccharomyces cerevisiae. Journal of Biological Chemistry 250 (1975) 1269-1274
    • (1975) Journal of Biological Chemistry , vol.250 , pp. 1269-1274
    • Poulson, R.1    Polglase, W.J.2
  • 16
    • 0029970569 scopus 로고    scopus 로고
    • Function of the [2Fe-2S] cluster in mammalian ferrochelatase: A possible role as a nitric oxide sensor
    • Sellers V.M., Johnson M.K., and Dailey H.A. Function of the [2Fe-2S] cluster in mammalian ferrochelatase: A possible role as a nitric oxide sensor. Biochemistry 35 (1996) 2699-2704
    • (1996) Biochemistry , vol.35 , pp. 2699-2704
    • Sellers, V.M.1    Johnson, M.K.2    Dailey, H.A.3
  • 18
    • 37349089753 scopus 로고    scopus 로고
    • Heme synthase (ferrochelatase) catalyzes the removal of iron from heme and demetalation of metalloporphyrins
    • Taketani S., Ishigaki M., Mizutani A., Uebayashi M., Numata M., Ohgari Y., et al. Heme synthase (ferrochelatase) catalyzes the removal of iron from heme and demetalation of metalloporphyrins. Biochemistry 46 (2007) 15054-15061
    • (2007) Biochemistry , vol.46 , pp. 15054-15061
    • Taketani, S.1    Ishigaki, M.2    Mizutani, A.3    Uebayashi, M.4    Numata, M.5    Ohgari, Y.6
  • 19
    • 60249095550 scopus 로고    scopus 로고
    • Quantitative determination of Zn protoporphyrin IX, heme and protoporphyrin IX in Parma ham by HPLC
    • Wakamatsu J., Odagiri H., Nishimura T., and Hattori A. Quantitative determination of Zn protoporphyrin IX, heme and protoporphyrin IX in Parma ham by HPLC. Meat Science 82 (2009) 139-142
    • (2009) Meat Science , vol.82 , pp. 139-142
    • Wakamatsu, J.1    Odagiri, H.2    Nishimura, T.3    Hattori, A.4
  • 20
    • 33847154036 scopus 로고    scopus 로고
    • Direct demonstration of the presence of zinc in the acetone-extractable red pigment from Parma ham
    • Wakamatsu J., Ito T., Nishimura T., and Hattori A. Direct demonstration of the presence of zinc in the acetone-extractable red pigment from Parma ham. Meat Science 76 (2007) 385-387
    • (2007) Meat Science , vol.76 , pp. 385-387
    • Wakamatsu, J.1    Ito, T.2    Nishimura, T.3    Hattori, A.4
  • 21
    • 0942267927 scopus 로고    scopus 로고
    • A Zn-porphyrin complex contributes to bright red color in Parma ham
    • Wakamatsu J., Nishimura T., and Hattori A. A Zn-porphyrin complex contributes to bright red color in Parma ham. Meat Science 67 (2004) 95-100
    • (2004) Meat Science , vol.67 , pp. 95-100
    • Wakamatsu, J.1    Nishimura, T.2    Hattori, A.3
  • 22
    • 33746667195 scopus 로고    scopus 로고
    • Observation of the distribution of Zn protoporphyrin IX (ZPP) in Parma ham by using purple LED and image analysis
    • Wakamatsu J., Odagiri H., Nishimura T., and Hattori A. Observation of the distribution of Zn protoporphyrin IX (ZPP) in Parma ham by using purple LED and image analysis. Meat Science 74 (2006) 594-599
    • (2006) Meat Science , vol.74 , pp. 594-599
    • Wakamatsu, J.1    Odagiri, H.2    Nishimura, T.3    Hattori, A.4
  • 23
    • 35648968599 scopus 로고    scopus 로고
    • Zn protoporphyrin IX is formed not from heme but from protoporphyrin IX
    • Wakamatsu J., Okui J., Hayashi N., Nishimura T., and Hattori A. Zn protoporphyrin IX is formed not from heme but from protoporphyrin IX. Meat Science 77 (2007) 580-586
    • (2007) Meat Science , vol.77 , pp. 580-586
    • Wakamatsu, J.1    Okui, J.2    Hayashi, N.3    Nishimura, T.4    Hattori, A.5
  • 24
    • 2942631427 scopus 로고    scopus 로고
    • Establishment of a model experiment system to elucidate the mechanism by which Zn-protoporphyrin IX is formed in nitrite-free dry-cured ham
    • Wakamatsu J., Okui J., Ikeda Y., Nishimura T., and Hattori A. Establishment of a model experiment system to elucidate the mechanism by which Zn-protoporphyrin IX is formed in nitrite-free dry-cured ham. Meat Science 68 (2004) 313-317
    • (2004) Meat Science , vol.68 , pp. 313-317
    • Wakamatsu, J.1    Okui, J.2    Ikeda, Y.3    Nishimura, T.4    Hattori, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.