메뉴 건너뛰기




Volumn 338, Issue 1, 2005, Pages 404-409

Heme-thiolate proteins

Author keywords

Cytochrome P450; Heme thiolate proteins; Thiolate anion

Indexed keywords

BACTERIAL ENZYME; CHLORIDE PEROXIDASE; CYSTATHIONINE BETA SYNTHASE; CYTOCHROME P450; ENZYME COOA; FUNGAL ENZYME; HEME REGULATED INITIATION FACTOR 2ALPHA KINASE; HEME THIOLATE PROTEIN; HEMOPROTEIN; ISOENZYME; NITRIC OXIDE SYNTHASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 27544511005     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.267     Document Type: Review
Times cited : (61)

References (39)
  • 1
    • 0001202995 scopus 로고
    • Pigments of rat liver microsomes
    • M. Klingenberg Pigments of rat liver microsomes Arch. Biochem. Biophys. 75 1958 376 386
    • (1958) Arch. Biochem. Biophys. , vol.75 , pp. 376-386
    • Klingenberg, M.1
  • 2
    • 0001045385 scopus 로고
    • A new cytochrome in liver microsomes
    • T. Omura, and R. Sato A new cytochrome in liver microsomes J. Biol. Chem. 237 1962 1375 1376
    • (1962) J. Biol. Chem. , vol.237 , pp. 1375-1376
    • Omura, T.1    Sato, R.2
  • 3
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes, I.Evidence for its hemoprotein nature
    • T. Omura, and R. Sato The carbon monoxide-binding pigment of liver microsomes, I.Evidence for its hemoprotein nature J. Biol. Chem. 239 1964 2370 2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 4
    • 3943085370 scopus 로고
    • An electron resonance study of microsomal electron transport
    • Y. Hashimoto, T. Yamano, and H.S. Mason An electron resonance study of microsomal electron transport J. Biol. Chem. 237 1962 3843 3844
    • (1962) J. Biol. Chem. , vol.237 , pp. 3843-3844
    • Hashimoto, Y.1    Yamano, T.2    Mason, H.S.3
  • 5
    • 0014216316 scopus 로고
    • An electron spin resonance study of microsomal Fex
    • K. Murakami, and H.S. Mason An electron spin resonance study of microsomal Fex J. Biol. Chem. 242 1967 1102 1110
    • (1967) J. Biol. Chem. , vol.242 , pp. 1102-1110
    • Murakami, K.1    Mason, H.S.2
  • 6
    • 0014196737 scopus 로고
    • Reconversion of detergent- and sulfhydryl reagent-produced P-420 to P-450 by polyols and glutathione
    • Y. Ichikawa, and T. Yamano Reconversion of detergent- and sulfhydryl reagent-produced P-420 to P-450 by polyols and glutathione Biochim.Biophys.Acta 131 1967 490 497
    • (1967) Biochim.Biophys.Acta , vol.131 , pp. 490-497
    • Ichikawa, Y.1    Yamano, T.2
  • 7
    • 0016325554 scopus 로고
    • A model compound study of the CO-adduct of cytochrome P-450
    • J.O. Stern, and J. Peisach A model compound study of the CO-adduct of cytochrome P-450 J. Biol. Chem. 249 1974 7495 7498
    • (1974) J. Biol. Chem. , vol.249 , pp. 7495-7498
    • Stern, J.O.1    Peisach, J.2
  • 8
    • 0042939577 scopus 로고
    • Molecular cloning and nucleotide sequence of cDNA for mRNA of mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex
    • K. Morohashi, Y. Fujii-Kuriyama, Y. Okada, K. Sogawa, T. Hirose, S. Inayama, and T. Omura Molecular cloning and nucleotide sequence of cDNA for mRNA of mitochondrial cytochrome P-450(SCC) of bovine adrenal cortex, Proc. Natl. Acad. Sci. USA 81 1984 4647 4651
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4647-4651
    • Morohashi, K.1    Fujii-Kuriyama, Y.2    Okada, Y.3    Sogawa, K.4    Hirose, T.5    Inayama, S.6    Omura, T.7
  • 10
    • 0015919594 scopus 로고
    • The P-450 nature of the carbon monoxide complex of ferrous chloroperoxidase
    • P.F. Hollenberg, and L.P. Hager The P-450 nature of the carbon monoxide complex of ferrous chloroperoxidase J. Biol. Chem. 248 1973 2630 2633
    • (1973) J. Biol. Chem. , vol.248 , pp. 2630-2633
    • Hollenberg, P.F.1    Hager, L.P.2
  • 13
    • 0017190901 scopus 로고
    • Isolation and properties of a new, soluble, hemoprotein (H-450) from pig liver
    • I.C. Kim, and W.C. Deal Isolation and properties of a new, soluble, hemoprotein (H-450) from pig liver Biochemistry 15 1976 4925 4930
    • (1976) Biochemistry , vol.15 , pp. 4925-4930
    • Kim, I.C.1    Deal, W.C.2
  • 14
    • 0021528407 scopus 로고
    • Hemoprotein H-450 identified as a form of cytochrome P-450 having an endogenous ligand at the 6th coordination position of the heme
    • T. Omura, H. Sadano, T. Hasegawa, Y. Yoshida, and S. Kominami Hemoprotein H-450 identified as a form of cytochrome P-450 having an endogenous ligand at the 6th coordination position of the heme J.Biochem. 96 1984 1491 1500
    • (1984) J.Biochem. , vol.96 , pp. 1491-1500
    • Omura, T.1    Sadano, H.2    Hasegawa, T.3    Yoshida, Y.4    Kominami, S.5
  • 15
    • 0025696047 scopus 로고
    • Molecular cloning and sequence analysis of cDNA coding for rat liver hemoprotein H-450
    • S. Ishihara, K. Morohashi, H. Sadano, S. Kawabata, O. Gotoh, and T. Omura Molecular cloning and sequence analysis of cDNA coding for rat liver hemoprotein H-450 J.Biochem. 108 1990 899 902
    • (1990) J.Biochem. , vol.108 , pp. 899-902
    • Ishihara, S.1    Morohashi, K.2    Sadano, H.3    Kawabata, S.4    Gotoh, O.5    Omura, T.6
  • 17
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P-450 type hemoprotein
    • K.A. White, and M.A. Marletta Nitric oxide synthase is a cytochrome P-450 type hemoprotein Biochemistry 31 1992 6627 6631
    • (1992) Biochemistry , vol.31 , pp. 6627-6631
    • White, K.A.1    Marletta, M.A.2
  • 18
    • 0026471538 scopus 로고
    • Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide
    • K. McMillan, D.S. Bredt, D.J. Hirsch, S.H. Snyder, J.E. Clark, and B.S.S. Masters Cloned, expressed rat cerebellar nitric oxide synthase contains stoichiometric amounts of heme, which binds carbon monoxide Proc.Natl.Acad.Sci. USA. 89 1992 11141 11145
    • (1992) Proc.Natl.Acad.Sci.USA. , vol.89 , pp. 11141-11145
    • McMillan, K.1    Bredt, D.S.2    Hirsch, D.J.3    Snyder, S.H.4    Clark, J.E.5    Masters, B.S.S.6
  • 19
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • D.S. Bredt, P.M. Hwang, C.E. Glatt, O. Lowenstein, R.R. Reed, and S.H. Snyder Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase Nature 351 1991 714 718
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, O.4    Reed, R.R.5    Snyder, S.H.6
  • 20
    • 0032475847 scopus 로고    scopus 로고
    • Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA
    • S. Aono, K. Ohkubo, T. Matsuo, and H. Nakajima Redox-controlled ligand exchange of the heme in the CO-sensing transcriptional activator CooA J. Biol. Chem. 273 1998 25757 25764
    • (1998) J. Biol. Chem. , vol.273 , pp. 25757-25764
    • Aono, S.1    Ohkubo, K.2    Matsuo, T.3    Nakajima, H.4
  • 21
    • 1942469554 scopus 로고    scopus 로고
    • Activation of heme-regulated eukaryotic initiation factor 2α kinase by nitric oxide is induced by the formation of a five-coordinated NO-heme complex
    • J. Igarawshi, A. Sato, T. Kitagawa, T. Yoshimura, S. Yamauchi, I. Sagami, and T. Shimizu Activation of heme-regulated eukaryotic initiation factor 2α kinase by nitric oxide is induced by the formation of a five-coordinated NO-heme complex J. Biol. Chem. 279 2004 15752 15762
    • (2004) J. Biol. Chem. , vol.279 , pp. 15752-15762
    • Igarawshi, J.1    Sato, A.2    Kitagawa, T.3    Yoshimura, T.4    Yamauchi, S.5    Sagami, I.6    Shimizu, T.7
  • 22
    • 0000747371 scopus 로고
    • The light reversible carbon monoxide inhibition of the steroid C21-hydroxylase system of the adrenal cortex
    • R.W. Estabrook, D.Y. Cooper, and O. Rosenthal The light reversible carbon monoxide inhibition of the steroid C21-hydroxylase system of the adrenal cortex Biochem.Z. 338 1963 741 755
    • (1963) Biochem.Z. , vol.338 , pp. 741-755
    • Estabrook, R.W.1    Cooper, D.Y.2    Rosenthal, O.3
  • 23
    • 0033616138 scopus 로고    scopus 로고
    • Forty years of cytochrome P450
    • T. Omura Forty years of cytochrome P450 Biochem. Biophys. Res. Commun. 266 1999 690 698
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 690-698
    • Omura, T.1
  • 26
    • 0022400306 scopus 로고
    • Isolation and characterization of thromboxane synthase from human platelets as a cytochrome P-450 enzyme
    • M. Haurand, and V. Ullrich Isolation and characterization of thromboxane synthase from human platelets as a cytochrome P-450 enzyme J. Biol. Chem. 260 1985 15059 15067
    • (1985) J. Biol. Chem. , vol.260 , pp. 15059-15067
    • Haurand, M.1    Ullrich, V.2
  • 27
    • 0027418338 scopus 로고
    • Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor
    • K. Nakahara, T. Tanimoto, K. Hatano, K. Usuda, and H. Shoun Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor J. Biol. Chem. 268 1993 8350 8355
    • (1993) J. Biol. Chem. , vol.268 , pp. 8350-8355
    • Nakahara, K.1    Tanimoto, T.2    Hatano, K.3    Usuda, K.4    Shoun, H.5
  • 29
    • 3142749051 scopus 로고    scopus 로고
    • Cystathionine β-synthase: Structure, function, regulation and location of homocystiuria-causing mutations
    • E.W. Miles, and J.P. Kraus Cystathionine β-synthase: Structure, function, regulation and location of homocystiuria-causing mutations J. Biol. Chem. 279 2004 29871 29874
    • (2004) J. Biol. Chem. , vol.279 , pp. 29871-29874
    • Miles, E.W.1    Kraus, J.P.2
  • 30
    • 0035421273 scopus 로고    scopus 로고
    • Structure of human cystathionine β-synthase; A unique pyridoxal 5'-phosphate-dependent heme protein
    • M. Meiyer, M. Janosik, V. Kery, J.P. Kraus, and P. Burkhard Structure of human cystathionine β-synthase; a unique pyridoxal 5'-phosphate-dependent heme protein EMBO J. 20 2001 3910 3916
    • (2001) EMBO J. , vol.20 , pp. 3910-3916
    • Meiyer, M.1    Janosik, M.2    Kery, V.3    Kraus, J.P.4    Burkhard, P.5
  • 31
    • 0034730104 scopus 로고    scopus 로고
    • Domain architecture of the heme- independent yeast cystathionine β-synthase provide insights into mechanisms of catalysis and regulation
    • K.H. Jhee, P. McPhie, and E.W. Miles Domain architecture of the heme- independent yeast cystathionine β-synthase provide insights into mechanisms of catalysis and regulation Biochemistry. 39 2000 10548 10556
    • (2000) Biochemistry. , vol.39 , pp. 10548-10556
    • Jhee, K.H.1    McPhie, P.2    Miles, E.W.3
  • 33
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties
    • T. Omura, and R. Sato The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties J. Biol. Chem. 239 1964 2379 2385
    • (1964) J. Biol. Chem. , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 34
    • 0030597287 scopus 로고    scopus 로고
    • A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodosprillum rubrum
    • S. Aono, H. Nakajima, K. Saito, and M. Okada A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodosprillum rubrum Biochem. Biophys. Res. Commun. 228 1996 752 756
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 752-756
    • Aono, S.1    Nakajima, H.2    Saito, K.3    Okada, M.4
  • 35
    • 0035831489 scopus 로고    scopus 로고
    • Redox properties and coordination structure of the heme in the CO-sensing transcription activator CooA
    • H. Nakajima, Y. Honma, T. Tawara, T. Kato, S. Park, H. Miyataka, Y. Shiro, and S. Aono Redox properties and coordination structure of the heme in the CO-sensing transcription activator CooA J. Biol. Chem. 276 2001 7055 7061
    • (2001) J. Biol. Chem. , vol.276 , pp. 7055-7061
    • Nakajima, H.1    Honma, Y.2    Tawara, T.3    Kato, T.4    Park, S.5    Miyataka, H.6    Shiro, Y.7    Aono, S.8
  • 37
    • 0022993474 scopus 로고
    • Activation of soluble guanylate cyclase by NO-hemoproteins involves NO-heme exchange
    • L.J. Ignarro, J.B. Adams, P.M. Horwitz, and K.S. Wood Activation of soluble guanylate cyclase by NO-hemoproteins involves NO-heme exchange J. Biol. Chem. 261 1986 4997 5002
    • (1986) J. Biol. Chem. , vol.261 , pp. 4997-5002
    • Ignarro, L.J.1    Adams, J.B.2    Horwitz, P.M.3    Wood, K.S.4
  • 39
    • 0025878267 scopus 로고
    • A hemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • M.A. Gilles-Gonzalez, G.S. Ditta, and D.R. Helinski A hemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti Nature 350 1991 170 172
    • (1991) Nature , vol.350 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.