메뉴 건너뛰기




Volumn 117, Issue 2, 1998, Pages 525-532

The NAD(P)H dehydrogenase in barley thylakoids is photoactivatable and uses NADPH as well as NADH

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0000272126     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.117.2.525     Document Type: Article
Times cited : (46)

References (17)
  • 1
    • 84989730062 scopus 로고
    • Structural and functional analysis of the reducing side of photosystem I
    • Andersen B, Koch B, Scheller HV (1992) Structural and functional analysis of the reducing side of photosystem I. Physiol Plant 84: 154-161
    • (1992) Physiol Plant , vol.84 , pp. 154-161
    • Andersen, B.1    Koch, B.2    Scheller, H.V.3
  • 2
    • 0030571582 scopus 로고    scopus 로고
    • Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P)H-dehydrogenase (complex I)
    • Appel J, Schulz R (1996) Sequence analysis of an operon of a NAD(P)-reducing nickel hydrogenase from the cyanobacterium Synechocystis sp. PCC 6803 gives additional evidence for direct coupling of the enzyme to NAD(P)H-dehydrogenase (complex I). Biochim Biophys Acta 1298: 141-147
    • (1996) Biochim Biophys Acta , vol.1298 , pp. 141-147
    • Appel, J.1    Schulz, R.2
  • 3
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts. Polyphenol oxidase in Beta vulgaris
    • Arnon DI (1949) Copper enzymes in isolated chloroplasts. Polyphenol oxidase in Beta vulgaris. Plant Physiol 24: 1-15
    • (1949) Plant Physiol , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 4
    • 0027191417 scopus 로고
    • Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803
    • Berger S, Ellersiek U, Kinzelt D, Steinmüller K (1993) Immunopurification of a subcomplex of the NAD(P)H-plastoquinone-oxidoreductase from the cyanobacterium Synechocystis sp. PCC6803. FEBS Lett 326: 246-250
    • (1993) FEBS Lett , vol.326 , pp. 246-250
    • Berger, S.1    Ellersiek, U.2    Kinzelt, D.3    Steinmüller, K.4
  • 5
    • 0000324745 scopus 로고    scopus 로고
    • Nitrate reductase biochemistry comes of age
    • Campbell WH (1996) Nitrate reductase biochemistry comes of age. Plant Physiol 111: 355-361
    • (1996) Plant Physiol , vol.111 , pp. 355-361
    • Campbell, W.H.1
  • 6
    • 0029142099 scopus 로고
    • Properties of a large complex with NADH dehydrogenase activity from barley thylakoids
    • Cuello J, Quiles MJ, Albacete ME, Sabater B (1995) Properties of a large complex with NADH dehydrogenase activity from barley thylakoids. Plant Cell Physiol 36: 265-271
    • (1995) Plant Cell Physiol , vol.36 , pp. 265-271
    • Cuello, J.1    Quiles, M.J.2    Albacete, M.E.3    Sabater, B.4
  • 7
    • 0343672139 scopus 로고
    • The purification of nicotinamide adenine dinucleotide and the kinetic effects of nucleotide impurities
    • Dalziel K (1963) The purification of nicotinamide adenine dinucleotide and the kinetic effects of nucleotide impurities. J Biol Chem 238: 1538-1543
    • (1963) J Biol Chem , vol.238 , pp. 1538-1543
    • Dalziel, K.1
  • 8
    • 0002739120 scopus 로고
    • Determination of total protein concentration
    • ELV Harris, S Angal, eds, Oxford University Press, New York
    • Dunn MJ (1989) Determination of total protein concentration. In ELV Harris, S Angal, eds, Protein Purification Methods: A Practical Approach. Oxford University Press, New York, pp 13-15
    • (1989) Protein Purification Methods: A Practical Approach , pp. 13-15
    • Dunn, M.J.1
  • 9
    • 0029059910 scopus 로고
    • The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts
    • Friedrich T, Steinmüller K, Weiss H (1995) The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts. FEBS Lett 367: 107-111
    • (1995) FEBS Lett , vol.367 , pp. 107-111
    • Friedrich, T.1    Steinmüller, K.2    Weiss, H.3
  • 10
    • 0001077124 scopus 로고
    • Characterization of the NAD(P)H-plastoquinone-oxidoreductase from maize thylakoid membranes
    • P Mathis, ed, Kluwer Academic Publishers, Dordrecht, The Netherlands
    • Funk E, Steinmüller K (1995) Characterization of the NAD(P)H-plastoquinone-oxidoreductase from maize thylakoid membranes. In P Mathis, ed, Photosynthesis: From Light to Biosphere, Vol 2. Kluwer Academic Publishers, Dordrecht, The Netherlands, pp 701-704
    • (1995) Photosynthesis: from Light to Biosphere , vol.2 , pp. 701-704
    • Funk, E.1    Steinmüller, K.2
  • 11
    • 0019974543 scopus 로고
    • Evidence for a membrane bound NADH-plastoquinone-oxidoreductase in Chlamydomonas reinhardtii CW-15
    • Godde D (1982) Evidence for a membrane bound NADH-plastoquinone-oxidoreductase in Chlamydomonas reinhardtii CW-15. Arch Microbiol 131: 197-202
    • (1982) Arch Microbiol , vol.131 , pp. 197-202
    • Godde, D.1
  • 12
    • 0019126116 scopus 로고
    • NADH as electron donor for the photosynthetic membrane of Chlamydomonas reinhardtii
    • Godde D, Trebst A (1980) NADH as electron donor for the photosynthetic membrane of Chlamydomonas reinhardtii. Arch Microbiol 127: 245-252
    • (1980) Arch Microbiol , vol.127 , pp. 245-252
    • Godde, D.1    Trebst, A.2
  • 13
    • 0030295294 scopus 로고    scopus 로고
    • The NADH-binding subunit of respiratory chain complex I is nuclear-encoded in plants and identified only in mitochondria
    • Grohman L, Rasmusson AG, Heiser V, Thieck O, Brennicke A (1996) The NADH-binding subunit of respiratory chain complex I is nuclear-encoded in plants and identified only in mitochondria. Plant J 10: 793-803
    • (1996) Plant J , vol.10 , pp. 793-803
    • Grohman, L.1    Rasmusson, A.G.2    Heiser, V.3    Thieck, O.4    Brennicke, A.5
  • 14
    • 77957014322 scopus 로고
    • Application of inhibitors and uncouplers for a study of oxidative phosphorylation
    • Slater EC (1967) Application of inhibitors and uncouplers for a study of oxidative phosphorylation. Methods Enzymol 10: 48-57
    • (1967) Methods Enzymol , vol.10 , pp. 48-57
    • Slater, E.C.1
  • 16
    • 0019558007 scopus 로고
    • New concepts on the role of ubiquinone in the mitochondrial respiratory chain
    • Trumpower BL (1981) New concepts on the role of ubiquinone in the mitochondrial respiratory chain. J Bioenerg Biomembr 13: 1-24
    • (1981) J Bioenerg Biomembr , vol.13 , pp. 1-24
    • Trumpower, B.L.1
  • 17
    • 0001944852 scopus 로고
    • PsaE is required for in vivo cyclic electron flow around photosystem I in the cyanobacterium Synechococcus sp. FCC 7002
    • Yu L, Zhao J, Mühlenhoff U, Bryant DA, Golbeck JH (1993) PsaE is required for in vivo cyclic electron flow around photosystem I in the cyanobacterium Synechococcus sp. FCC 7002. Plant Physiol 103: 171-180
    • (1993) Plant Physiol , vol.103 , pp. 171-180
    • Yu, L.1    Zhao, J.2    Mühlenhoff, U.3    Bryant, D.A.4    Golbeck, J.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.