메뉴 건너뛰기




Volumn 48, Issue 40, 2009, Pages 9556-9568

Biophysical characterization of the iron in mitochondria from Atm1p-depleted Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; AEROBIC CELLS; ANAEROBIC CELLS; BIOPHYSICAL CHARACTERIZATION; CLUSTER ASSEMBLY; CYTOSOLIC; CYTOSOLS; ELECTRONIC ABSORPTION SPECTROSCOPY; FRATAXIN; INNER MEMBRANES; IRON METABOLISM; IRON PHOSPHATES; IRON-SULFUR CLUSTERS; NONHEME; OXIDATIVE DAMAGE; REACTIVE OXYGEN SPECIES; SACCHAROMYCES CEREVISIAE; SSBAUER SPECTROSCOPY;

EID: 70350054608     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901110n     Document Type: Article
Times cited : (80)

References (47)
  • 1
    • 0025267366 scopus 로고
    • The ferrochelatase from Saccharomyces cerevisiae - Sequence, disruption, and expression of its structural gene Hem15
    • Labbebois, R. (1990) The ferrochelatase from Saccharomyces cerevisiae - Sequence, disruption, and expression of its structural gene Hem15. J. Biol. Chem. 265, 7278-7283.
    • (1990) J. Biol. Chem. , vol.265 , pp. 7278-7283
    • Labbebois, R.1
  • 2
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill, R., and Mühlenhoff, U. (2008) Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 77, 669-700.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 3
    • 0028855545 scopus 로고
    • An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast
    • Leighton, J., and Schatz, G. (1995) An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast. EMBO J. 14, 188-195.
    • (1995) EMBO J. , vol.14 , pp. 188-195
    • Leighton, J.1    Schatz, G.2
  • 4
    • 33646876880 scopus 로고    scopus 로고
    • Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds
    • Kuhnke, G., Neumann, K., Mühlenhoff, U., and Lill, R. (2006) Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds. Mol. Membr. Biol. 23, 173-184.
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 173-184
    • Kuhnke, G.1    Neumann, K.2    Mühlenhoff, U.3    Lill, R.4
  • 5
    • 43749114744 scopus 로고    scopus 로고
    • Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis
    • Hausmann, A., Samans, B., Lill, R., and Mühlenhoff, U. (2008) Cellular and mitochondrial remodeling upon defects in iron-sulfur protein biogenesis. J. Biol. Chem. 283, 8318-8330.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8318-8330
    • Hausmann, A.1    Samans, B.2    Lill, R.3    Mühlenhoff, U.4
  • 6
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transport Atm1p is required for mitochondrial iron homeostasis
    • DOI 10.1016/S0014-5793(97)01414-2, PII S0014579397014142
    • Kispal, G., Csere, P., Guiard, B., and Lill, R. (1997) The ABC transporter Atm1p is required for mitochondrial iron homeostasis. FEBS Lett. 418, 346-350. (Pubitemid 27515954)
    • (1997) FEBS Letters , vol.418 , Issue.3 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 7
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • DOI 10.1093/emboj/18.14.3981
    • Kispal, G., Csere, P., Prohl, C., and Lill, R. (1999) The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18, 3981-3989. (Pubitemid 29335851)
    • (1999) EMBO Journal , vol.18 , Issue.14 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 8
    • 0020739930 scopus 로고
    • Heme regulates transcription of the Cyc1 gene of S. cerevisiae via an upstream activation site
    • Guarente, L., and Mason, T. (1983) Heme regulates transcription of the Cyc1 gene of S. cerevisiae via an upstream activation site. Cell 32, 1279-1286.
    • (1983) Cell , vol.32 , pp. 1279-1286
    • Guarente, L.1    Mason, T.2
  • 9
    • 3142722152 scopus 로고    scopus 로고
    • The heme synthesis defect of mutants impaired in mitochondrial ironsulfur protein biogenesis is caused by reversible inhibition of ferrochelatase
    • Lange, H., Mühlenhoff, U., Denzel, M., Kispal, G., and Lill, R. (2004) The heme synthesis defect of mutants impaired in mitochondrial ironsulfur protein biogenesis is caused by reversible inhibition of ferrochelatase. J. Biol. Chem. 279, 29101-29108.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29101-29108
    • Lange, H.1    Mühlenhoff, U.2    Denzel, M.3    Kispal, G.4    Lill, R.5
  • 11
  • 13
    • 15444371876 scopus 로고    scopus 로고
    • Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis
    • Rutherford, J. C., Ojeda, L., Balk, J., Mühlenhoff, U., Lill, R., and Winge, D. R. (2005) Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis. J. Biol. Chem. 280, 10135-10140.
    • (2005) J. Biol. Chem. , vol.280 , pp. 10135-10140
    • Rutherford, J.C.1    Ojeda, L.2    Balk, J.3    Mühlenhoff, U.4    Lill, R.5    Winge, D.R.6
  • 14
    • 21244449583 scopus 로고    scopus 로고
    • A mitochondrial half-size ABC transporter is involved in cadmium tolerance in Chlamydomonas reinhardtii
    • DOI 10.1111/j.1365-3040.2005.01335.x
    • Hanikenne, M., Motte, P., Wu, M. C. S., Wang, T., Loppes, R., and Matagne, R. F. (2005) A mitochondrial half-size ABC transporter is involved in cadmium tolerance in Chlamydomonas reinhardtii. Plant Cell Environ. 28, 863-873. (Pubitemid 40886094)
    • (2005) Plant, Cell and Environment , vol.28 , Issue.7 , pp. 863-873
    • Hanikenne, M.1    Motte, P.2    Wu, M.C.S.3    Wang, T.4    Loppes, R.5    Matagne, R.F.6
  • 15
    • 0032414310 scopus 로고    scopus 로고
    • Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
    • DOI 10.1016/S0014-5793(98)01560-9, PII S0014579398015609
    • Csere, P., Lill, R., and Kispal, G. (1998) Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p. FEBS Lett. 441, 266-270. (Pubitemid 29027908)
    • (1998) FEBS Letters , vol.441 , Issue.2 , pp. 266-270
    • Csere, P.1    Lill, R.2    Kispal, G.3
  • 16
    • 0034329310 scopus 로고    scopus 로고
    • Human ABC7 transporter: Gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation
    • Bekri, S., Kispal, G., Lange, H., Fitzsimons, E., Tolmie, J., Lill, R., and Bishop, D. F. (2000) Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation. Blood 96, 3256-3264. (Pubitemid 30815240)
    • (2000) Blood , vol.96 , Issue.9 , pp. 3256-3264
    • Bekri, S.1    Kispal, G.2    Lange, H.3    Fitzsimons, E.4    Tolmie, J.5    Lill, R.6    Bishop, D.F.7
  • 17
    • 51249119361 scopus 로고    scopus 로고
    • Recent advances in the understanding of inherited sideroblastic anaemia
    • Camaschella, C. (2008) Recent advances in the understanding of inherited sideroblastic anaemia. Br. J. Hamaetol. 143, 27-38.
    • (2008) Br. J. Hamaetol. , vol.143 , pp. 27-38
    • Camaschella, C.1
  • 18
    • 34147158934 scopus 로고    scopus 로고
    • Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis
    • DOI 10.1182/blood-2006-04-015768
    • Pondarre, C., Campagna, D. R., Antiochos, B., Sikorski, L., Mulhern, H., and Fleming, M. D. (2007) Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis. Blood 109, 3567-3569. (Pubitemid 46572551)
    • (2007) Blood , vol.109 , Issue.8 , pp. 3567-3569
    • Pondarre, C.1    Campagna, D.R.2    Antiochos, B.3    Sikorski, L.4    Mulhern, H.5    Fleming, M.D.6
  • 19
    • 34548445911 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and Mössbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae
    • Hudder, B. N., Morales, J. G., Stubna, A., Münck, E., Hendrich, M. P., and Lindahl, P. A. (2007) Electron paramagnetic resonance and Mössbauer spectroscopy of intact mitochondria from respiring Saccharomyces cerevisiae. J. Biol. Inorg. Chem. 12, 1029-1053.
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 1029-1053
    • Hudder, B.N.1    Morales, J.G.2    Stubna, A.3    Münck, E.4    Hendrich, M.P.5    Lindahl, P.A.6
  • 20
    • 63449089627 scopus 로고    scopus 로고
    • Isolation of Saccharomyces cerevisiae mitochondria for Mössbauer, EPR, and electronic absorption spectroscopic analyses
    • Lindahl, P., Morales, J. G., Miao, R., and Holmes-Hampton, G. (2009) Isolation of Saccharomyces cerevisiae mitochondria for Mössbauer, EPR, and electronic absorption spectroscopic analyses. Methods Enzymol. 456, 267-285.
    • (2009) Methods Enzymol. , vol.456 , pp. 267-285
    • Lindahl, P.1    Morales, J.G.2    Miao, R.3    Holmes-Hampton, G.4
  • 21
    • 0033621156 scopus 로고    scopus 로고
    • Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae
    • Schilke, B., Voisine, C., Beinert, H., and Craig, E. (1999) Evidence for a conserved system for iron metabolism in the mitochondria of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 96, 10206-10211.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10206-10211
    • Schilke, B.1    Voisine, C.2    Beinert, H.3    Craig, E.4
  • 22
    • 0024198152 scopus 로고
    • Isopropylmalate dehydratase from yeast
    • Kohlhaw, G. B. (1988) Isopropylmalate dehydratase from yeast. Methods Enzymol. 166, 423-429.
    • (1988) Methods Enzymol. , vol.166 , pp. 423-429
    • Kohlhaw, G.B.1
  • 23
    • 0027254848 scopus 로고
    • Assay of succinate-dehydrogenase activity by a colorimetric-continuous method using iodonitrotetrazolium chloride as electron-acceptor
    • Munujos, P., Collcanti, J., Gonzalezsastre, F., and Gella, F. J. (1993) Assay of succinate-dehydrogenase activity by a colorimetric-continuous method using iodonitrotetrazolium chloride as electron-acceptor. Anal. Biochem. 212, 506-509.
    • (1993) Anal. Biochem. , vol.212 , pp. 506-509
    • Munujos, P.1    Collcanti, J.2    Gonzalezsastre, F.3    Gella, F.J.4
  • 24
    • 33644947727 scopus 로고    scopus 로고
    • Colorimetric assay for the quantitation of iron in yeast
    • Tamarit, J., Irazusta, V., Moreno-Cermeno, A., and Ros, J. (2006) Colorimetric assay for the quantitation of iron in yeast. Anal. Biochem. 351, 149-151.
    • (2006) Anal. Biochem. , vol.351 , pp. 149-151
    • Tamarit, J.1    Irazusta, V.2    Moreno-Cermeno, A.3    Ros, J.4
  • 25
    • 0001555957 scopus 로고    scopus 로고
    • Multiple-scattering x-ray-absorption fine-structure Debye-Waller factor calculations
    • Poiarkova, A. V., and Rehr, J. J. (1999) Multiple-scattering x-ray-absorption fine-structure Debye-Waller factor calculations. Phys. Rev. B 59, 948-957.
    • (1999) Phys. Rev. B , vol.59 , pp. 948-957
    • Poiarkova, A.V.1    Rehr, J.J.2
  • 26
    • 0014440704 scopus 로고
    • Promitochondria of anaerobically grown yeast. 3. Morphology
    • Plattner, H., and Schatz, G. (1969) Promitochondria of anaerobically grown yeast. 3. Morphology. Biochemistry 8, 339-343.
    • (1969) Biochemistry , vol.8 , pp. 339-343
    • Plattner, H.1    Schatz, G.2
  • 27
    • 0036135461 scopus 로고    scopus 로고
    • Genomic analyses of anaerobically induced genes in Saccharomyces cerevisiae: Functional roles of Rox1 and other factors in mediating the anoxic response
    • DOI 10.1128/JB.184.1.250-265.2002
    • Kwast, K. E., Lai, L. C., Menda, N., James, D. T., Aref, S., and Burke, P. V. (2002) Genomic analyses of anaerobically induced genes in Saccharomyces cerevisiae: Functional roles of Rox1 and other factors in mediating the anoxic response. J. Bacteriol. 184, 250-265. (Pubitemid 34003306)
    • (2002) Journal of Bacteriology , vol.184 , Issue.1 , pp. 250-265
    • Kwast, K.E.1    Lai, L.-C.2    Menda, N.3    James III, D.T.4    Aref, S.5    Burke, P.V.6
  • 28
    • 0014440624 scopus 로고
    • Promitochondria of anaerobically grown yeast. 2. Lipid composition
    • Paltauf, F., and Schatz, G. (1969) Promitochondria of anaerobically grown yeast. 2. Lipid composition. Biochemistry 8, 335-339.
    • (1969) Biochemistry , vol.8 , pp. 335-339
    • Paltauf, F.1    Schatz, G.2
  • 29
    • 0142248154 scopus 로고    scopus 로고
    • Role of the non-respiratory pathways in the utilization of molecular oxygen by Saccharomyces cerevisiae
    • DOI 10.1002/yea.1026
    • Rosenfeld, E., and Beauvoit, B. (2003) Role of the non-respiratory pathways in the utilization of molecular oxygen by Saccharomyces cerevisiae. Yeast 20, 1115-1144. (Pubitemid 37309272)
    • (2003) Yeast , vol.20 , Issue.13 , pp. 1115-1144
    • Rosenfeld, E.1    Beauvoit, B.2
  • 30
    • 0037155866 scopus 로고    scopus 로고
    • Mitochondrial ferredoxin is required for heme A synthesis in Saccharomyces cerevisiae
    • Barros, M. H., Nobrega, F. G., and Tzagoloff, A. (2002) Mitochondrial ferredoxin is required for heme A synthesis in Saccharomyces cerevisiae. J. Biol. Chem. 277, 9997-10002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9997-10002
    • Barros, M.H.1    Nobrega, F.G.2    Tzagoloff, A.3
  • 32
    • 0032571374 scopus 로고    scopus 로고
    • Regulation of high affinity iron uptake in the yeast Saccharomyces cerevisiae - Role of dioxygen and Fe(II)
    • Hassett, R. F., Romeo, A. M., and Kosman, D. J. (1998) Regulation of high affinity iron uptake in the yeast Saccharomyces cerevisiae - Role of dioxygen and Fe(II). J. Biol. Chem. 273, 7628-7636.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7628-7636
    • Hassett, R.F.1    Romeo, A.M.2    Kosman, D.J.3
  • 33
    • 0036302227 scopus 로고    scopus 로고
    • Regulation of Saccharomyces cerevisiae FET4 by oxygen and iron
    • Jensen, L. T., and Culotta, V. C. (2002) Regulation of Saccharomyces cerevisiae FET4 by oxygen and iron. J. Mol. Biol. 318, 251-260.
    • (2002) J. Mol. Biol. , vol.318 , pp. 251-260
    • Jensen, L.T.1    Culotta, V.C.2
  • 34
    • 0037072773 scopus 로고    scopus 로고
    • Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen
    • Waters, B. M., and Eide, D. J. (2002) Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen. J. Biol. Chem. 277, 33749-33757.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33749-33757
    • Waters, B.M.1    Eide, D.J.2
  • 35
    • 34147165135 scopus 로고    scopus 로고
    • RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload
    • DOI 10.1182/blood-2006-08-041632
    • Cavadini, P., Biasiotto, G., Poli, M., Levi, S., Verardi, R., Zanella, I., Derosas, M., Ingrassia, R., Corrado, M., and Arosio, P. (2007) RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload. Blood 109, 3552-3559. (Pubitemid 46572549)
    • (2007) Blood , vol.109 , Issue.8 , pp. 3552-3559
    • Cavadini, P.1    Biasiotto, G.2    Poli, M.3    Levi, S.4    Verardi, R.5    Zanella, I.6    Derosas, M.7    Ingrassia, R.8    Corrado, M.9    Arosio, P.10
  • 36
    • 59249102083 scopus 로고    scopus 로고
    • The wanderings of a free radical
    • Halliwell, B. (2009) The wanderings of a free radical. Free Radical Biol. Med. 46, 531-542.
    • (2009) Free Radical Biol. Med. , vol.46 , pp. 531-542
    • Halliwell, B.1
  • 37
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • Imlay, J. A. (2006) Iron-sulphur clusters and the problem with oxygen. Mol. Microbiol. 59, 1073-1082.
    • (2006) Mol. Microbiol. , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 38
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria; Arequirement for ATP, NADH, and reduced iron
    • Mühlenhoff, U., Richhardt, N., Gerber, J., and Lill, R. (2002) Characterization of iron-sulfur protein assembly in isolated mitochondria; Arequirement for ATP, NADH, and reduced iron. J. Biol. Chem. 277, 29810-29816.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29810-29816
    • Mühlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 39
    • 34547602992 scopus 로고    scopus 로고
    • Assessment of chelatable mitochondrial iron by using mitochondrion- Selective fluorescent iron indicators with different iron-binding affinities
    • DOI 10.1002/cbic.200600311
    • Rauen, U., Springer, A., Weisheit, D., Petrat, F., Korth, H. G., de Groot, H., and Sustmann, R. (2007) Assessment of chelatable mitochondrial iron by using mitochondrion-selective fluorescent iron indicators with different iron-binding affinities. ChemBioChem 8, 341-352. (Pubitemid 47194515)
    • (2007) ChemBioChem , vol.8 , Issue.3 , pp. 341-352
    • Rauen, U.1    Springer, A.2    Weisheit, D.3    Petrat, F.4    Korth, H.-G.5    De Groot, H.6    Sustmann, R.7
  • 41
    • 0000529845 scopus 로고
    • Modeling hydrolysis at dinuclear iron centers
    • Wilkinson, E. C., Dong, Y. H., and Que, L. (1994) Modeling hydrolysis at dinuclear iron centers. J. Am. Chem. Soc. 116, 8394-8395.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8394-8395
    • Wilkinson, E.C.1    Dong, Y.H.2    Que, L.3
  • 42
    • 0033516467 scopus 로고    scopus 로고
    • Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria
    • Lange, H., Kispal, G., and Lill, R. (1999) Mechanism of iron transport to the site of heme synthesis inside yeast mitochondria. J. Biol. Chem. 274, 18989-18996.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18989-18996
    • Lange, H.1    Kispal, G.2    Lill, R.3
  • 43
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms
    • Lill, R., and Mühlenhoff, U. (2006) Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms. Annu. Rev. Cell. Dev. Biol. 22, 457-486.
    • (2006) Annu. Rev. Cell. Dev. Biol. , vol.22 , pp. 457-486
    • Lill, R.1    Mühlenhoff, U.2
  • 44
    • 0001853405 scopus 로고    scopus 로고
    • The role of the mitochondrion in cellular iron homeostasis
    • DOI 10.1016/S1567-7249(01)00004-6, PII S1567724901000046
    • Schueck, N. D., Woontner, M., and Koeller, D. M. (2001) The role of the mitochondrion in cellular iron homeostasis. Mitochondrion 1, 51-60. (Pubitemid 33586020)
    • (2001) Mitochondrion , vol.1 , Issue.1 , pp. 51-60
    • Schueck, N.D.1    Woontner, M.2    Koeller, D.M.3
  • 45
    • 34447527359 scopus 로고    scopus 로고
    • Mitochondrial ATP-binding cassette proteins
    • Burke, M. A., and Ardehali, H. (2007) Mitochondrial ATP-binding cassette proteins. Transl. Res. 150, 73-80.
    • (2007) Transl. Res. , vol.150 , pp. 73-80
    • Burke, M.A.1    Ardehali, H.2
  • 46
    • 34547116659 scopus 로고    scopus 로고
    • Functional characterization of AtATM1, AtATM2, and AtATM3, a subfamily of Arabidopsis half-molecule ATP-binding cassette transporters implicated in iron homeostasis
    • Chen, S., Sanchez-Fernandez, R., Lyver, E. R., Dancis, A., and Rea, P. A. (2007) Functional characterization of AtATM1, AtATM2, and AtATM3, a subfamily of Arabidopsis half-molecule ATP-binding cassette transporters implicated in iron homeostasis. J. Biol. Chem. 282, 21561-21571.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21561-21571
    • Chen, S.1    Sanchez-Fernandez, R.2    Lyver, E.R.3    Dancis, A.4    Rea, P.A.5
  • 47
    • 0000056384 scopus 로고
    • Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes. 2. Refined distances and other enzymes
    • Liu, W. T., and Thorp, H. H. (1993) Bond valence sum analysis of metal-ligand bond lengths in metalloenzymes and model complexes. 2. Refined distances and other enzymes. Inorg. Chem. 32, 4102-4105.
    • (1993) Inorg. Chem. , vol.32 , pp. 4102-4105
    • Liu, W.T.1    Thorp, H.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.