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Volumn 109, Issue 15, 2012, Pages 5583-5587

Unification of reaction pathway and kinetic scheme for N 2 reduction catalyzed by nitrogenase

Author keywords

EPR; ESEEM; Non Kramers

Indexed keywords

HYDRAZINE; NITROGEN; NITROGENASE;

EID: 84859592982     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1202197109     Document Type: Article
Times cited : (57)

References (27)
  • 2
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess BK, Lowe DJ (1996) Mechanism of molybdenum nitrogenase. Chem Rev 96:2983-3011. (Pubitemid 126641125)
    • (1996) Chemical Reviews , vol.96 , Issue.7 , pp. 2983-3011
    • Burgess, B.K.1    Lowe, D.J.2
  • 4
    • 66149110298 scopus 로고    scopus 로고
    • Climbing nitrogenase: Towards the mechanism of enzymatic nitrogen fixation
    • Hoffman BM, Dean DR, Seefeldt LC (2009) Climbing nitrogenase: Towards the mechanism of enzymatic nitrogen fixation. Acc Chem Res 42:609-619.
    • (2009) Acc Chem Res , vol.42 , pp. 609-619
    • Hoffman, B.M.1    Dean, D.R.2    Seefeldt, L.C.3
  • 5
    • 0001442098 scopus 로고
    • Kinetics and mechanism of the nitrogenase enzyme system
    • Molybdenum Enzymes, ed TG Spiro (Wiley-Interscience, New York)
    • Thorneley RNF, Lowe DJ (1985) Kinetics and mechanism of the nitrogenase enzyme system. Molybdenum Enzymes, ed TG Spiro (Wiley-Interscience, New York), Metal Ions in Biology, 7, pp 89-116.
    • (1985) Metal Ions in Biology , vol.7 , pp. 89-116
    • Thorneley, R.N.F.1    Lowe, D.J.2
  • 6
    • 0035942982 scopus 로고    scopus 로고
    • Duplication and extension of the Thorneley and Lowe kinetic model for Klebsiella pneumoniae nitrogenase catalysis using a MATHEMATICA software platform
    • DOI 10.1016/S0301-4622(01)00182-X, PII S030146220100182X
    • Wilson PE, Nyborg AC, Watt GD (2001) Duplication and extension of the Thorneley and Lowe kinetic model for Klebsiella pneumoniae nitrogenase catalysis using a MATHEMATICA software platform. Biophys Chem 91:281-304. (Pubitemid 32707884)
    • (2001) Biophysical Chemistry , vol.91 , Issue.3 , pp. 281-304
    • Wilson, P.E.1    Nyborg, A.C.2    Watt, G.D.3
  • 7
    • 0017807020 scopus 로고
    • Biological nitrogen fixation by way of an enzyme-bound dinitrogen-hydride intermediate
    • DOI 10.1038/272557a0
    • Thorneley RNF, Eady RR, Lowe DJ (1978) Biological nitrogen fixation by way of an enzyme-bound dinitrogen-hydride intermediate. Nature 272:557-558. (Pubitemid 8312316)
    • (1978) Nature , vol.272 , Issue.5653 , pp. 557-558
    • Thorneley, R.N.F.1    Eady, R.R.2    Lowe, D.J.3
  • 10
    • 0024728608 scopus 로고
    • Integer-spin electron paramagnetic resonance of iron proteins
    • Hendrich MP, Debrunner PG (1989) Integer-spin electron paramagnetic resonance of iron proteins. Biophys J 56:489-506.
    • (1989) Biophys J , vol.56 , pp. 489-506
    • Hendrich, M.P.1    Debrunner, P.G.2
  • 11
    • 0027330259 scopus 로고
    • Combining Mössbauer spectroscopy with integer spin electron paramagnetic resonance
    • Münck E, Surerus K, Hendrich MP (1993) Combining Mössbauer spectroscopy with integer spin electron paramagnetic resonance. Methods Enzymol Part C 227:463-479.
    • (1993) Methods Enzymol Part C , vol.227 , pp. 463-479
    • Münck, E.1    Surerus, K.2    Hendrich, M.P.3
  • 12
    • 0028066240 scopus 로고
    • ESEEM and ENDOR magnetic resonance studies of the non-Kramers doublet in the integer-spin diiron(II) forms of two methane monooxygenase hydroxylases and hemerythrin azide
    • Hoffman BM, et al. (1994) ESEEM and ENDOR magnetic resonance studies of the non-Kramers doublet in the integer-spin diiron(II) forms of two methane monooxygenase hydroxylases and hemerythrin azide. J Am Chem Soc 116:6023-6024.
    • (1994) J Am Chem Soc , vol.116 , pp. 6023-6024
    • Hoffman, B.M.1
  • 13
    • 0035916919 scopus 로고    scopus 로고
    • Electron paramagnetic resonance analysis of different Azotobacter vinelandii nitrogenase MoFe-protein conformations generated during enzyme turnover: Evidence for S = 3/2 spin states from reduced MoFe-protein intermediates
    • DOI 10.1021/bi0012686
    • Fisher K, Newton WE, Lowe DJ (2001) Electron paramagnetic resonance analysis of different Azotobacter vinelandii nitrogenase MoFe-protein conformations generated during enzyme turnover: Evidence for S = 3/2 spin states from reduced MoFe-protein intermediates. Biochemistry 40:3333-3339. (Pubitemid 32221635)
    • (2001) Biochemistry , vol.40 , Issue.11 , pp. 3333-3339
    • Fisher, K.1    Newton, W.E.2    Lowe, D.J.3
  • 14
    • 0000799274 scopus 로고
    • Spin Hamiltonian for even-electron systems having even multiplicity
    • Griffith JS (1963) Spin Hamiltonian for even-electron systems having even multiplicity. Phys Rev 132:316-319.
    • (1963) Phys Rev , vol.132 , pp. 316-319
    • Griffith, J.S.1
  • 15
    • 0001349725 scopus 로고
    • ENDOR and ESEEM of a non-Kramers doublet in an integer-spin system
    • Hoffman BM (1994) ENDOR and ESEEM of a non-Kramers doublet in an integer-spin system. J Phys Chem 98:11657-11665.
    • (1994) J Phys Chem , vol.98 , pp. 11657-11665
    • Hoffman, B.M.1
  • 17
    • 0033797352 scopus 로고    scopus 로고
    • How important is parallel-mode EPR in electron spin echo envelope modulation studies of non-Kramers systems?
    • Doan PE, Hoffman BM (2000) How important is parallel-mode EPR in electron spin echo envelope modulation studies of non-Kramers systems? Inorg Chim Acta 297:400-403.
    • (2000) Inorg Chim Acta , vol.297 , pp. 400-403
    • Doan, P.E.1    Hoffman, B.M.2
  • 23
    • 0019135266 scopus 로고
    • Hydrazine as a substrate and inhibitor of Azotobacter vinelandii nitrogenase
    • Davis LC (1980) Hydrazine as a substrate and inhibitor of Azotobacter vinelandii nitrogenase. Arch Biochem Biophys 204:270-276.
    • (1980) Arch Biochem Biophys , vol.204 , pp. 270-276
    • Davis, L.C.1
  • 25
    • 33751232674 scopus 로고    scopus 로고
    • 3)-derived species bound to the nitrogenase active-site FeMo cofactor: Implications for mechanism
    • 3)-derived species bound to the nitrogenase active-site FeMo cofactor: Implications for mechanism. Proc Natl Acad Sci USA 103:17113-17118.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17113-17118
    • Barney, B.M.1
  • 27
    • 62649111228 scopus 로고    scopus 로고
    • Structure of the nucleotide radical formed during reaction of CDP/TTP with the E441Q-a2b2 of E. coli ribonucleotide reductase
    • Zipse H, et al. (2009) Structure of the nucleotide radical formed during reaction of CDP/TTP with the E441Q-a2b2 of E. coli ribonucleotide reductase. J Am Chem Soc 131:200-211.
    • (2009) J Am Chem Soc , vol.131 , pp. 200-211
    • Zipse, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.