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Volumn 50, Issue 49, 2011, Pages 10743-10750

Erratum: Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: Investigation of kinetics and requirement for an external electron donor (Biochemistry (2011) 50:49 (10743-10750). DOI: 10.1021/bi2012417);Oxygen-independent alkane formation by non-heme iron-dependent cyanobacterial aldehyde decarbonylase: Investigation of kinetics and requirement for an external electron donor

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDES; CARBOXYLATION; ENZYMES; PARAFFINS;

EID: 82955240582     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300837j     Document Type: Erratum
Times cited : (63)

References (22)
  • 1
    • 0031128012 scopus 로고    scopus 로고
    • The glossy1 locus of maize and an epidermis-specific cDNA from Kleinia odora define a class of receptor-like proteins required for the normal accumulation of cuticular waxes
    • Hansen, J. D., Pyee, J., Xia, Y., Wen, T. J., Robertson, D. S., Kolattukudy, P. E., Nikolau, B. J., and Schnable, P. S. (1997) The glossy1 locus of maize and an epidermis-specific cDNA from Kleinia odora define a class of receptor-like proteins required for the normal accumulation of cuticular waxes Plant Physiol. 113, 1091-1100 (Pubitemid 27215555)
    • (1997) Plant Physiology , vol.113 , Issue.4 , pp. 1091-1100
    • Hansen, J.D.1    Pyee, J.2    Xia, Y.3    Wen, T.-J.4    Robertson, D.S.5    Kolattukudy, P.E.6    Nikolau, B.J.7    Schnable, P.S.8
  • 2
    • 0037211529 scopus 로고    scopus 로고
    • Biosynthesis and secretion of plant cuticular wax
    • DOI 10.1016/S0163-7827(02)00045-0, PII S0163782702000450
    • Kunst, L. and Samuels, A. L. (2003) Biosynthesis and secretion of plant cuticular wax Prog. Lipid Res. 42, 51-80 (Pubitemid 35418208)
    • (2003) Progress in Lipid Research , vol.42 , Issue.1 , pp. 51-80
    • Kunst, L.1    Samuels, A.L.2
  • 3
    • 0000915278 scopus 로고
    • Enhancement of diapausing flesh fly puparia with additional hydrocarbons and evidence for alkane biosynthesis by a decarbonylation mechanism
    • Yoder, J. A., Denlinger, D. L., Dennis, M. W., and Kolattukudy, P. E. (1992) Enhancement of diapausing flesh fly puparia with additional hydrocarbons and evidence for alkane biosynthesis by a decarbonylation mechanism Insect Biochem. Mol. Biol. 22, 237-243
    • (1992) Insect Biochem. Mol. Biol. , vol.22 , pp. 237-243
    • Yoder, J.A.1    Denlinger, D.L.2    Dennis, M.W.3    Kolattukudy, P.E.4
  • 5
    • 0023828762 scopus 로고
    • Microsomal preparation from an animal tissue catalyzes release of carbon monoxide from a fatty aldehyde to generate an alkane
    • Cheesbrough, T. M. and Kolattukudy, P. E. (1988) Microsomal preparation from an animal tissue catalyzes release of carbon monoxide from a fatty aldehyde to Generate an Alkane J. Biol. Chem. 263, 2738-2743 (Pubitemid 18062919)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.6 , pp. 2738-2743
    • Cheesbrough, T.M.1    Kolattukudy, P.E.2
  • 6
    • 0025889976 scopus 로고
    • Alkane biosynthesis by decarbonylation of aldehyde catalyzed by a microsomal preparation from Botryococcus braunii
    • Dennis, M. W. and Kolattukudy, P. E. (1991) Alkane biosynthesis by decarbonylation of aldehyde catalyzed by a microsomal preparation from Botryococcus braunii Arch. Biochem. Biophys. 287, 268-275
    • (1991) Arch. Biochem. Biophys. , vol.287 , pp. 268-275
    • Dennis, M.W.1    Kolattukudy, P.E.2
  • 7
    • 0031127392 scopus 로고    scopus 로고
    • Resolution and purification of an aldehyde-generating and an alcohol- generating fatty acyl-CoA reductase from pea leaves (Pisum sativum L.)
    • DOI 10.1006/abbi.1997.9932
    • Vioque, J. and Kolattukudy, P. E. (1997) Resolution and purification of an aldehyde-generating and an alcohol-generating fatty acyl-CoA reductase from pea leaves (Pisum sativum L) Arch. Biochem. Biophys. 340, 64-72 (Pubitemid 27200275)
    • (1997) Archives of Biochemistry and Biophysics , vol.340 , Issue.1 , pp. 64-72
    • Vioque, J.1    Kolattukudy, P.E.2
  • 8
    • 0021520992 scopus 로고
    • Alkane biosynthesis by decarbonylation of aldehydes catalyzed by a particulate preparation from Pisum sativum
    • Cheesbrough, T. M. and Kolattukudy, P. E. (1984) Alkane biosynthesis by decarbonylation of aldehydes catalyzed by a particulate preparation from Pisum sativum Proc. Natl. Acad. Sci. U. S. A. 81, 6613-6617
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 6613-6617
    • Cheesbrough, T.M.1    Kolattukudy, P.E.2
  • 9
    • 0026764128 scopus 로고
    • A cobalt-porphyrin enzyme converts a fatty aldehyde to a hydrocarbon and CO
    • Dennis, M. and Kolattukudy, P. E. (1992) A cobalt-porphyrin enzyme converts a fatty aldehyde to a hydrocarbon and CO Proc. Natl. Acad. Sci. U. S. A. 89, 5306-5310
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 5306-5310
    • Dennis, M.1    Kolattukudy, P.E.2
  • 11
    • 0034657291 scopus 로고    scopus 로고
    • Solubilization, partial purification, and characterization of a fatty aldehyde decarbonylase from a higher plant, Pisum sativum
    • DOI 10.1006/abbi.2000.1798
    • Schneider-Belhaddad, F. and Kolattukudy, P. (2000) Solubilization, partial purification, and characterization of a fatty aldehyde decarbonylase from a higher plant, Pisum sativum Arch. Biochem. Biophys. 377, 341-349 (Pubitemid 30331896)
    • (2000) Archives of Biochemistry and Biophysics , vol.377 , Issue.2 , pp. 341-349
    • Schneider-Belhaddad, F.1    Kolattukudy, P.2
  • 12
    • 79960638391 scopus 로고    scopus 로고
    • Oxygen-independent decarbonylation of aldehydes by cyano-bacterial aldehyde decarbonylase: A new reaction of di-iron enzymes
    • Das, D., Eser, B. E., Han, J., Sciore, A., and Marsh, E. N. G. (2011) Oxygen-independent decarbonylation of aldehydes by cyano-bacterial aldehyde decarbonylase: a new reaction of di-iron enzymes Angew. Chem., Int. Ed. 50, 7148-7152
    • (2011) Angew. Chem., Int. Ed. , vol.50 , pp. 7148-7152
    • Das, D.1    Eser, B.E.2    Han, J.3    Sciore, A.4    Marsh, E.N.G.5
  • 13
    • 79952588441 scopus 로고    scopus 로고
    • Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a ayanobacterial aldehyde decarbonylase
    • Warui, D. M., Li, N., Norgaard, H., Krebs, C., Bollinger, J. M., and Booker, S. J. (2011) Detection of formate, rather than carbon monoxide, as the stoichiometric coproduct in conversion of fatty aldehydes to alkanes by a ayanobacterial aldehyde decarbonylase J. Am. Chem. Soc. 133, 3316-3319
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3316-3319
    • Warui, D.M.1    Li, N.2    Norgaard, H.3    Krebs, C.4    Bollinger, J.M.5    Booker, S.J.6
  • 14
    • 0037560872 scopus 로고    scopus 로고
    • Mechanistic studies on the hydroxylation of methane by methane monooxygenase
    • Baik, M. H., Newcomb, M., Friesner, R. A., and Lippard, S. J. (2003) Mechanistic studies on the hydroxylation of methane by methane monooxygenase Chem. Rev. 103, 2385-2419
    • (2003) Chem. Rev. , vol.103 , pp. 2385-2419
    • Baik, M.H.1    Newcomb, M.2    Friesner, R.A.3    Lippard, S.J.4
  • 15
    • 0038208381 scopus 로고    scopus 로고
    • Radical initiation in the class i ribonucleotide reductase: Long-range proton-coupled electron transfer?
    • Stubbe, J., Nocera, D. G., Yee, C. S., and Chang, M. C. Y. (2003) Radical initiation in the class I ribonucleotide reductase: Long-range proton-coupled electron transfer? Chem. Rev. 103, 2167-2201
    • (2003) Chem. Rev. , vol.103 , pp. 2167-2201
    • Stubbe, J.1    Nocera, D.G.2    Yee, C.S.3    Chang, M.C.Y.4
  • 16
    • 79954995511 scopus 로고    scopus 로고
    • Conversion of fatty aldehydes to alka(e)nes and foramte by a cyanobacterial aldehyde decarbonylase: Crypric redox by an unusual dimetal oxygenase
    • Li, N., Norgaard, H., Warui, D. M., Booker, S. J., Krebs, C., and Bollinger, J. M. (2011) Conversion of fatty aldehydes to alka(e)nes and foramte by a cyanobacterial aldehyde decarbonylase: crypric redox by an unusual dimetal oxygenase J. Am. Chem. Soc. 133, 7148-7152
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7148-7152
    • Li, N.1    Norgaard, H.2    Warui, D.M.3    Booker, S.J.4    Krebs, C.5    Bollinger, J.M.6
  • 17
    • 65549089961 scopus 로고    scopus 로고
    • Purification, characterization, and potential bacterial wax production role of an NADPH-dependent fatty aldehyde reductase from Marinobacter aquaeolei VT8
    • Wahlen, B. D., Oswald, W. S., Seefeldt, L. C., and Barney, B. M. (2009) Purification, characterization, and potential bacterial wax production role of an NADPH-dependent fatty aldehyde reductase from Marinobacter aquaeolei VT8 Appl. Environ. Microbiol. 75, 2758-2764
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 2758-2764
    • Wahlen, B.D.1    Oswald, W.S.2    Seefeldt, L.C.3    Barney, B.M.4
  • 18
    • 0000098903 scopus 로고
    • Spectroscopic characteristics and some chemical properties of N-methylphenazinium methyl sulfate (phenazine methosulfate) and pyocyanine at the semiquidnoid oxidation level
    • Zaugg, W. S. (1964) Spectroscopic characteristics and some chemical properties of N-methylphenazinium methyl sulfate (phenazine methosulfate) and pyocyanine at the semiquidnoid oxidation level J. Biol. Chem. 239, 3964-3970
    • (1964) J. Biol. Chem. , vol.239 , pp. 3964-3970
    • Zaugg, W.S.1
  • 19
    • 81155161902 scopus 로고    scopus 로고
    • Cyanobacterial genomics for ecology and biotechnology
    • Hess, W. R. (2011) Cyanobacterial genomics for ecology and biotechnology Curr. Opin. Microbiol. 14, 608-614
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 608-614
    • Hess, W.R.1
  • 20
    • 0029582722 scopus 로고
    • Molecular characterization of the CER1 gene of Arabidopsis involved in epicuticular wax biosynthesis and pollen fertility
    • DOI 10.1105/tpc.7.12.2115
    • Aarts, M. G. M., Keijzer, C. J., Stiekema, W. J., and Pereira, A. (1995) Molecular characterization of the CER1 gene of arabidopsis involved in epicuticular wax biosynthesis and pollen fertility Plant Cell 7, 2115-2127 (Pubitemid 2615570)
    • (1995) Plant Cell , vol.7 , Issue.12 , pp. 2115-2127
    • Aarts, M.G.1    Keijzer, C.J.2    Stiekema, W.J.3    Pereira, A.4
  • 21
    • 0031128388 scopus 로고    scopus 로고
    • Characterization of a structurally and functionally diverged acyl-acyl carrier protein desaturase from milkweed seed
    • DOI 10.1023/A:1005821007291
    • Cahoon, E. B., Coughlan, S. J., and Shanklin, J. (1997) Characterization of a structurally and functionally diverged acyl-acyl carrier protein desaturase from milkweed seed Plant Mol. Biol. 33, 1105-1110 (Pubitemid 27235663)
    • (1997) Plant Molecular Biology , vol.33 , Issue.6 , pp. 1105-1110
    • Cahoon, E.B.1    Coughlan, S.J.2    Shanklin, J.3
  • 22
    • 0032091048 scopus 로고    scopus 로고
    • A determinant of substrate specificity predicted from the Acyl-Acyl carrier protein desaturase of developing cat's claw seed
    • Cahoon, E. B., Shah, S., Shanklin, J., and Browse, J. (1998) A determinant of substrate specificity predicted from the acyl-acyl carrier protein desaturase of developing cat's claw seed Plant Physiol. 117, 593-598 (Pubitemid 128652832)
    • (1998) Plant Physiology , vol.117 , Issue.2 , pp. 593-598
    • Cahoon, E.B.1    Shah, S.2    Shanklin, J.3    Browse, J.4


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