메뉴 건너뛰기




Volumn 766, Issue , 2011, Pages 3-7

Historic Overview of Nitrogenase Research

Author keywords

Biological nitrogen fixation; cell free extracts; nitrogenase; purification; x ray crystallography

Indexed keywords

NITROGENASE;

EID: 80052958833     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-194-9_1     Document Type: Chapter
Times cited : (23)

References (30)
  • 1
    • 0009822813 scopus 로고
    • Unter-suchungen über die Stickstoffnährung der Gramineen und Leguminosen
    • Hellriegel H, Wilfarth H (1888) Unter-suchungen über die Stickstoffnährung der Gramineen und Leguminosen. Beil Z Ver dt ZuchInd, 1–234
    • (1888) Beil Z Ver Dt Zuchind , pp. 1-234
    • Hellriegel, H.1    Wilfarth, H.2
  • 2
    • 85139123917 scopus 로고    scopus 로고
    • Beijerinck MW (1888) Die Bakterien der Papilionaceen-Knölchen. Bot Ztg 46:725–735; 741–750; 757–771; 781–790; 797–804
    • Beijerinck MW (1888) Die Bakterien der Papilionaceen-Knölchen. Bot Ztg 46:725–735; 741–750; 757–771; 781–790; 797–804
    • (2001)
  • 3
    • 0000273970 scopus 로고
    • Sur l’assimilation de l’azote gaseux de l’atmosphère par les microbes
    • Winogradsky S (1893) Sur l’assimilation de l’azote gaseux de l’atmosphère par les microbes. C r hedb Séanc Acad Sci Paris 116:1385–1388
    • (1893) C R Hedb Séanc Acad Sci Paris , vol.116 , pp. 1385-1388
    • Winogradsky, S.1
  • 4
    • 0039779547 scopus 로고
    • Über oligoni-trophile Mikroben
    • Beijerinck MW (1901) Über oligoni-trophile Mikroben. ZentBl Bakt ParasitKde 7:561–582
    • (1901) Zentbl Bakt Parasitkde , vol.7 , pp. 561-582
    • Beijerinck, M.W.1
  • 5
    • 14444277958 scopus 로고
    • On the fixation of air nitrogen through Azotobacter
    • Meyerhof O, Burk D (1928) On the fixation of air nitrogen through Azotobacter. Z Phys Chem 139:117–142
    • (1928) Z Phys Chem , vol.139 , pp. 117-142
    • Meyerhof, O.1    Burk, D.2
  • 6
    • 0001481801 scopus 로고
    • Molybdän als Katalysator bei der biologischen Stickstoffbindung
    • Bortels H (1930) Molybdän als Katalysator bei der biologischen Stickstoffbindung. Arch Mikrobiol 1:333–342
    • (1930) Arch Mikrobiol , vol.1 , pp. 333-342
    • Bortels, H.1
  • 7
    • 80052922242 scopus 로고
    • Distribution of isotopic nitrogen in Azotobacter vinelandii
    • Burris H (1942) Distribution of isotopic nitrogen in Azotobacter vinelandii. J Biol Chem 143:509–517
    • (1942) J Biol Chem , vol.143 , pp. 509-517
    • Burris, H.1
  • 8
    • 50549172892 scopus 로고
    • Nitrogen fixation in cell-free extracts of Clostridium pasteurianum
    • Carnahan JE, Mortenson LE, Mower HF et al (1960) Nitrogen fixation in cell-free extracts of Clostridium pasteurianum. Biochim Biophys Acta 38:188–189
    • (1960) Biochim Biophys Acta , vol.38 , pp. 188-189
    • Carnahan, J.E.1    Mortenson, L.E.2    Mower, H.F.3
  • 9
    • 0014502573 scopus 로고
    • Progress in the biochemistry of nitrogen fixation
    • Burris RH (1969) Progress in the biochemistry of nitrogen fixation. Proc R Soc Lond B Biol Sci 172:339–354
    • (1969) Proc R Soc Lond B Biol Sci , vol.172 , pp. 339-354
    • Burris, R.H.1
  • 10
    • 0013773668 scopus 로고
    • Nitrogen fixation: Cell-free system with extracts of Azotobacter
    • Bulen WA, Burns RC, LeComte JR (1964) Nitrogen fixation: cell-free system with extracts of Azotobacter. Biochem Biophys Res Commun 17:265–271
    • (1964) Biochem Biophys Res Commun , vol.17 , pp. 265-271
    • Bulen, W.A.1    Burns, R.C.2    Lecomte, J.R.3
  • 11
    • 0006736112 scopus 로고
    • Nitrogen fixation: Hydrogensulfite as electron donor with cell-free preparations of Azotobacter vinelandii and Rhodospirillum rubrum
    • Bulen WA, Burns RC, Lecomte JR (1965) Nitrogen fixation: hydrogensulfite as electron donor with cell-free preparations of Azotobacter vinelandii and Rhodospirillum rubrum. Proc Natl Acad Sci USA 53: 532–539
    • (1965) Proc Natl Acad Sci USA , vol.53 , pp. 532-539
    • Bulen, W.A.1    Burns, R.C.2    Lecomte, J.R.3
  • 13
    • 0014220774 scopus 로고
    • Purification, metal composition and properties of molybdoferredoxin and azoferredoxin, two of the components of the nitrogen-fixing system of Clostridium pasteurianum
    • Mortenson LE, Morris JA, Jeng DY (1967) Purification, metal composition and properties of molybdoferredoxin and azoferredoxin, two of the components of the nitrogen-fixing system of Clostridium pasteurianum. Biochim Biophys Acta 141:516–522
    • (1967) Biochim Biophys Acta , vol.141 , pp. 516-522
    • Mortenson, L.E.1    Morris, J.A.2    Jeng, D.Y.3
  • 14
    • 0001442098 scopus 로고
    • Kinetics and mechanism of the nitrogenase enzyme system
    • (ed) Molybdenum Enzymes, Wiley, New York, NY
    • Thorneley RNF, Lowe DJ (1985) Kinetics and mechanism of the nitrogenase enzyme system. In: Spiro, TG (ed) Molybdenum Enzymes, pp. 221–284. Wiley, New York, NY
    • (1985) Spiro, TG , pp. 221-284
    • Thorneley, R.N.F.1    Lowe, D.J.2
  • 15
    • 0026662162 scopus 로고
    • Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii
    • Georgiadis MM, Komiya H, Chakrabarti P et al (1992) Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii. Science 257:1653–1659
    • (1992) Science , vol.257 , pp. 1653-1659
    • Georgiadis, M.M.1    Komiya, H.2    Chakrabarti, P.3
  • 16
    • 0026705527 scopus 로고
    • Structural models for the metal centers in the nitrogenase molybdenum-iron protein
    • Kim J, Rees DC (1992) Structural models for the metal centers in the nitrogenase molybdenum-iron protein. Science 257:1677–1682
    • (1992) Science , vol.257 , pp. 1677-1682
    • Kim, J.1    Rees, D.C.2
  • 17
    • 0027159222 scopus 로고
    • The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures
    • Chan MK, Kim J, Rees DC (1993) The nitrogenase FeMo-cofactor and P-cluster pair: 2.2 A resolution structures. Science 260:792–794
    • (1993) Science , vol.260 , pp. 792-794
    • Chan, M.K.1    Kim, J.2    Rees, D.C.3
  • 18
    • 0037389661 scopus 로고    scopus 로고
    • Speculative synthetic chemistry and the nitrogenase problem
    • Lee SC, Holm RH (2003) Speculative synthetic chemistry and the nitrogenase problem. Proc Natl Acad Sci USA 100: 3595–3600
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 3595-3600
    • Lee, S.C.1    Holm, R.H.2
  • 19
    • 1542334620 scopus 로고    scopus 로고
    • The clusters of nitrogenase: Synthetic methodology in the construction of weak-field clusters
    • Lee SC, Holm RH (2004) The clusters of nitrogenase: synthetic methodology in the construction of weak-field clusters. Chem Rev 104:1135–1158
    • (2004) Chem Rev , vol.104 , pp. 1135-1158
    • Lee, S.C.1    Holm, R.H.2
  • 20
    • 64849111092 scopus 로고    scopus 로고
    • Biomimetic chemistry of iron, nickel, molybdenum, and tungsten in sulfur-ligated protein sites
    • Groysman S, Holm RH (2009) Biomimetic chemistry of iron, nickel, molybdenum, and tungsten in sulfur-ligated protein sites. Biochemistry 48:2310–2320
    • (2009) Biochemistry , vol.48 , pp. 2310-2320
    • Groysman, S.1    Holm, R.H.2
  • 21
    • 0028188777 scopus 로고
    • Fe/S and Fe/Mo/S clusters as speculative models for the metal centers in uncommon Fe/S proteins and the Fe/Mo protein of the nitrogenases
    • Coucouvanis D (1994) Fe/S and Fe/Mo/S clusters as speculative models for the metal centers in uncommon Fe/S proteins and the Fe/Mo protein of the nitrogenases. Adv Inorg Biochem 9:75–122
    • (1994) Adv Inorg Biochem , vol.9 , pp. 75-122
    • Coucouvanis, D.1
  • 22
    • 0037427293 scopus 로고    scopus 로고
    • Synthesis of the P-cluster inorganic core of nitrogenases
    • Ohki Y, Sunada Y, Honda M, Katada M, Tatsumi K (2003) Synthesis of the P-cluster inorganic core of nitrogenases. J Am Chem Soc 125:4052–4053
    • (2003) J am Chem Soc , vol.125 , pp. 4052-4053
    • Ohki, Y.1    Sunada, Y.2    Honda, M.3    Katada, M.4    Tatsumi, K.5
  • 23
    • 51649102776 scopus 로고    scopus 로고
    • Electronic structure and reactivity of three-coordinate iron complexes
    • Holland PL (2008) Electronic structure and reactivity of three-coordinate iron complexes. Acc Chem Res 41:905–914
    • (2008) Acc Chem Res , vol.41 , pp. 905-914
    • Holland, P.L.1
  • 26
    • 33751256876 scopus 로고    scopus 로고
    • 2? A mechanistic overview of biological nitrogen fixation
    • 2? A mechanistic overview of biological nitrogen fixation. Proc Natl Acad Sci USA 103: 17088–17093
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17088-17093
    • Howard, J.B.1    Rees, D.C.2
  • 27
    • 0000703950 scopus 로고    scopus 로고
    • Mechanism of molybdenum nitrogenase
    • Burgess BK, Lowe DJ (1996) Mechanism of molybdenum nitrogenase. Chem Rev 96:2983–3012
    • (1996) Chem Rev , vol.96 , pp. 2983-3012
    • Burgess, B.K.1    Lowe, D.J.2
  • 29
    • 1542304548 scopus 로고    scopus 로고
    • Formation and insertion of the nitrogenase iron-molybdenum cofactor
    • Dos Santos PC, Dean DR, Hu Y, Ribbe MW (2004) Formation and insertion of the nitrogenase iron-molybdenum cofactor. Chem Rev 104:1159–1173
    • (2004) Chem Rev , vol.104 , pp. 1159-1173
    • Dos Santos, P.C.1    Dean, D.R.2    Hu, Y.3    Ribbe, M.W.4
  • 30
    • 68949107281 scopus 로고    scopus 로고
    • Molybdenum cofactors, enzymes and pathways
    • Schwarz G, Mendel RR, Ribbe MW (2009) Molybdenum cofactors, enzymes and pathways. Nature 460:839–847
    • (2009) Nature , vol.460 , pp. 839-847
    • Schwarz, G.1    Mendel, R.R.2    Ribbe, M.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.