메뉴 건너뛰기




Volumn 196, Issue 4, 2014, Pages 850-858

Nonredundant roles for cytochrome c2 and two high-potential iron-sulfur proteins in the photoferrotroph rhodopseudomonas palustris TIE-1

Author keywords

[No Author keywords available]

Indexed keywords

COBALT; CYTOCHROME C2; DIVALENT CATION; FERROUS ION; IRON SULFUR PROTEIN; NICKEL;

EID: 84893120256     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00843-13     Document Type: Article
Times cited : (43)

References (39)
  • 1
    • 0041859232 scopus 로고    scopus 로고
    • Discovery and characterization of electron transfer proteins in the photosynthetic bacteria
    • Meyer TE, Cusanovich MA. 2003. Discovery and characterization of electron transfer proteins in the photosynthetic bacteria. Photosynth. Res. 76:111-126. http://dx.doi.org/10.1023/A:1024910323089.
    • (2003) Photosynth. Res. , vol.76 , pp. 111-126
    • Meyer, T.E.1    Cusanovich, M.A.2
  • 2
    • 0028879888 scopus 로고
    • Influence of charge and polarity on the redox potentials of high-potential iron-sulfur proteins: evidence for the existence of two groups
    • Heering HA, Bulsink BM, Hagen WR, Meyer TE. 1995. Influence of charge and polarity on the redox potentials of high-potential iron-sulfur proteins: evidence for the existence of two groups. Biochemistry 34: 14675-14686. http://dx.doi.org/10.1021/bi00045a008.
    • (1995) Biochemistry , vol.34 , pp. 14675-14686
    • Heering, H.A.1    Bulsink, B.M.2    Hagen, W.R.3    Meyer, T.E.4
  • 3
    • 38549169460 scopus 로고    scopus 로고
    • Development of a heme protein structure-electrochemical function database
    • Database Issue
    • Reedy CJ, Elvekrog MM, Gibney BR. 2008. Development of a heme protein structure-electrochemical function database. Nucleic Acids Res. 36(Database Issue):D307-D313. http://dx.doi.org/10.1093/nar/gkm814.
    • (2008) Nucleic Acids Res. , vol.36
    • Reedy, C.J.1    Elvekrog, M.M.2    Gibney, B.R.3
  • 4
    • 10744232309 scopus 로고    scopus 로고
    • Amino acid sequences and distribution of high-potential iron-sulfur proteins that donate electrons to the photosynthetic reaction center in phototropic proteobacteria
    • Van Driessche G, Vandenberghe I, Devreese B, Samyn B, Meyer TE, Leigh R, Cusanovich MA, Bartsch RG, Fischer U, Van Beeumen JJ. 2003. Amino acid sequences and distribution of high-potential iron-sulfur proteins that donate electrons to the photosynthetic reaction center in phototropic proteobacteria. J. Mol. Evol. 57:181-199. http://dx.doi.org /10.1007/s00239-003-2465-y.
    • (2003) J. Mol. Evol. , vol.57 , pp. 181-199
    • Van Driessche, G.1    Vandenberghe, I.2    Devreese, B.3    Samyn, B.4    Meyer, T.E.5    Leigh, R.6    Cusanovich, M.A.7    Bartsch, R.G.8    Fischer, U.9    Van Beeumen, J.J.10
  • 5
    • 14744281354 scopus 로고    scopus 로고
    • Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier
    • Lieutaud C, Alric J, Bauzan M, Nitschke W, Schoepp-Cothenet B. 2005. Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier. Proc. Natl. Acad. Sci. U. S. A. 102:3260-3265. http://dx.doi.org/10.1073 /pnas.0407768102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3260-3265
    • Lieutaud, C.1    Alric, J.2    Bauzan, M.3    Nitschke, W.4    Schoepp-Cothenet, B.5
  • 6
    • 0031925488 scopus 로고    scopus 로고
    • Role of HiPIP as electron donor to the RC-bound cytochrome in photosynthetic purple bacteria
    • Menin L, Gaillard J, Parot P, Schoepp B, Nitschke W, Vermeglio A. 1998. Role of HiPIP as electron donor to the RC-bound cytochrome in photosynthetic purple bacteria. Photosynth. Res. 55:343-348. http://dx .doi.org/10.1023/A:1005989900756.
    • (1998) Photosynth. Res. , vol.55 , pp. 343-348
    • Menin, L.1    Gaillard, J.2    Parot, P.3    Schoepp, B.4    Nitschke, W.5    Vermeglio, A.6
  • 7
    • 0030767268 scopus 로고    scopus 로고
    • Photoinduced cyclic electron transfer in Rhodocyclus tenuis cells: participation of HiPIP or cyt c8 depending on the ambient redox potential
    • Menin L, Schoepp B, Parot P, Vermeglio A. 1997. Photoinduced cyclic electron transfer in Rhodocyclus tenuis cells: participation of HiPIP or cyt c8 depending on the ambient redox potential. Biochemistry 36:12183-12188. http://dx.doi.org/10.1021/bi971163b.
    • (1997) Biochemistry , vol.36 , pp. 12183-12188
    • Menin, L.1    Schoepp, B.2    Parot, P.3    Vermeglio, A.4
  • 8
    • 0346850581 scopus 로고    scopus 로고
    • Interactions between cytochrome c(2) and photosynthetic reaction center from Rhodobacter sphaeroides: changes in binding affinity and electron transfer rate due to mutation of interfacial hydrophobic residues are strongly correlated
    • Gong XM, Paddock ML, Okamura MY. 2003. Interactions between cytochrome c(2) and photosynthetic reaction center from Rhodobacter sphaeroides: changes in binding affinity and electron transfer rate due to mutation of interfacial hydrophobic residues are strongly correlated. Biochemistry 42:14492-14500. http://dx.doi.org/10.1021/bi035603c.
    • (2003) Biochemistry , vol.42 , pp. 14492-14500
    • Gong, X.M.1    Paddock, M.L.2    Okamura, M.Y.3
  • 9
    • 70349773181 scopus 로고    scopus 로고
    • Cytochrome c(4) can be involved in the photosynthetic electron transfer system in the purple bacterium Rubrivivax gelatinosus
    • Ohmine M, Matsuura K, Shimada K, Alric J, Vermeglio A, Nagashima KVP. 2009. Cytochrome c(4) can be involved in the photosynthetic electron transfer system in the purple bacterium Rubrivivax gelatinosus. Biochemistry 48:9132-9139. http://dx.doi.org/10.1021/bi901202m.
    • (2009) Biochemistry , vol.48 , pp. 9132-9139
    • Ohmine, M.1    Matsuura, K.2    Shimada, K.3    Alric, J.4    Vermeglio, A.5    Nagashima, K.V.P.6
  • 10
    • 0030011855 scopus 로고    scopus 로고
    • Kinetics of photo-induced electron transfer from highpotential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentans
    • Hochkoeppler A, Zannoni D, Ciurli S, Meyer TE, Cusanovich MA, Tollin G. 1996. Kinetics of photo-induced electron transfer from highpotential iron-sulfur protein to the photosynthetic reaction center of the purple phototroph Rhodoferax fermentans. Proc. Natl. Acad. Sci. U. S. A. 93:6998-7002. http://dx.doi.org/10.1073/pnas.93.14.6998.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 6998-7002
    • Hochkoeppler, A.1    Zannoni, D.2    Ciurli, S.3    Meyer, T.E.4    Cusanovich, M.A.5    Tollin, G.6
  • 11
    • 0029088458 scopus 로고
    • In vivo participation of a high potential iron-sulfur protein as electron donor to the photochemical reaction center of Rubrivivax gelatinosus
    • Schoepp B, Parot P, Menin L, Gaillard J, Richaud P, Vermeglio A. 1995. In vivo participation of a high potential iron-sulfur protein as electron donor to the photochemical reaction center of Rubrivivax gelatinosus. Biochemistry 34:11736-11742. http://dx.doi.org/10.1021/bi00037a010.
    • (1995) Biochemistry , vol.34 , pp. 11736-11742
    • Schoepp, B.1    Parot, P.2    Menin, L.3    Gaillard, J.4    Richaud, P.5    Vermeglio, A.6
  • 12
    • 84858710013 scopus 로고    scopus 로고
    • Photo-induced electron transfer in intact cells of Rubrivivax gelatinosus mutants deleted in the RC-bound tetraheme cytochrome: insight into evolution of photosynthetic electron transport
    • Vermeglio A, Nagashima S, Alric J, Arnoux P, Nagashima KV. 2012. Photo-induced electron transfer in intact cells of Rubrivivax gelatinosus mutants deleted in the RC-bound tetraheme cytochrome: insight into evolution of photosynthetic electron transport. Biochim. Biophys. Acta 1817:689-696. http://dx.doi.org/10.1016/j.bbabio.2012.01.011.
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 689-696
    • Vermeglio, A.1    Nagashima, S.2    Alric, J.3    Arnoux, P.4    Nagashima, K.V.5
  • 13
    • 23744498874 scopus 로고    scopus 로고
    • Isolation and characterization of a genetically tractable photoautotrophic Fe(II)-oxidizing bacterium, Rhodopseudomonas palustris strain TIE-1
    • Jiao Y, Kappler A, Croal LR, Newman DK. 2005. Isolation and characterization of a genetically tractable photoautotrophic Fe(II)-oxidizing bacterium, Rhodopseudomonas palustris strain TIE-1. Appl. Environ. Microbiol. 71:4487-4496. http://dx.doi.org/10.1128/AEM.71.8.4487-4496.2005.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4487-4496
    • Jiao, Y.1    Kappler, A.2    Croal, L.R.3    Newman, D.K.4
  • 14
    • 33947358262 scopus 로고    scopus 로고
    • The pio operon is essential for phototrophic Fe(II) oxidation in Rhodopseudomonas palustris TIE-1
    • Jiao Y, Newman DK. 2007. The pio operon is essential for phototrophic Fe(II) oxidation in Rhodopseudomonas palustris TIE-1. J. Bacteriol. 189: 1765-1773. http://dx.doi.org/10.1128/JB.00776-06.
    • (2007) J. Bacteriol. , vol.189 , pp. 1765-1773
    • Jiao, Y.1    Newman, D.K.2
  • 15
    • 1642528965 scopus 로고    scopus 로고
    • Iron isotope fractionation by Fe(II)-oxidizing photoautotrophic bacteria
    • Croal LR, Johnson CM, Beard BL, Newman DK. 2004. Iron isotope fractionation by Fe(II)-oxidizing photoautotrophic bacteria. Geochim. Cosmochim. Acta 68:1227-1242. http://dx.doi.org/10.1016/j.gca.2003.09 .011.
    • (2004) Geochim. Cosmochim. Acta , vol.68 , pp. 1227-1242
    • Croal, L.R.1    Johnson, C.M.2    Beard, B.L.3    Newman, D.K.4
  • 16
    • 33746045692 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae-based molecular tool kit for manipulation of genes from gram-negative bacteria
    • Shanks RMQ, Caiazza NC, Hinsa SM, Toutain CM, O'Toole GA. 2006. Saccharomyces cerevisiae-based molecular tool kit for manipulation of genes from gram-negative bacteria. Appl. Environ. Microbiol. 72:5027-5036. http://dx.doi.org/10.1128/AEM.00682-06.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 5027-5036
    • Shanks, R.M.Q.1    Caiazza, N.C.2    Hinsa, S.M.3    Toutain, C.M.4    O'Toole, G.A.5
  • 18
    • 68549123548 scopus 로고    scopus 로고
    • SOAS: a free program to analyze electrochemical data and other one-dimensional signals
    • Fourmond V, Hoke K, Heering HA, Baffert C, Leroux F, Bertrand P, Leger C. 2009. SOAS: a free program to analyze electrochemical data and other one-dimensional signals. Bioelectrochemistry 76:141-147. http://dx .doi.org/10.1016/j.bioelechem.2009.02.010.
    • (2009) Bioelectrochemistry , vol.76 , pp. 141-147
    • Fourmond, V.1    Hoke, K.2    Heering, H.A.3    Baffert, C.4    Leroux, F.5    Bertrand, P.6    Leger, C.7
  • 19
    • 33750622183 scopus 로고
    • Cytochromes: bacterial
    • Bartsch RG. 1971. Cytochromes: bacterial. Methods Enzymol. 23:344-363.
    • (1971) Methods Enzymol. , vol.23 , pp. 344-363
    • Bartsch, R.G.1
  • 20
    • 0015220486 scopus 로고
    • Oxidation-reduction potential dependence of the interaction of cytochromes, bacteriochlorophyll and carotenoids at 11°K in chromatophores of Chromatium D and Rhodopseudomonas gelatinosa
    • Dutton PL. 1971. Oxidation-reduction potential dependence of the interaction of cytochromes, bacteriochlorophyll and carotenoids at 11°K in chromatophores of Chromatium D and Rhodopseudomonas gelatinosa. Biochim. Biophys. Acta 226:63-80. http://dx.doi.org/10.1016/0005-2728 (71)90178-2.
    • (1971) Biochim. Biophys. Acta , vol.226 , pp. 63-80
    • Dutton, P.L.1
  • 21
    • 78650286309 scopus 로고    scopus 로고
    • The cytochrome c(8) involved in the nitrite reduction pathway acts also as electron donor to the photosynthetic reaction center in Rubrivivax gelatinosus
    • Nagashima S, Shimada K, Vermeglio A, Nagashima KV. 2011. The cytochrome c(8) involved in the nitrite reduction pathway acts also as electron donor to the photosynthetic reaction center in Rubrivivax gelatinosus. Biochim. Biophys. Acta 1807:189-196. http://dx.doi.org/10.1016 /j.bbabio.2010.10.020.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 189-196
    • Nagashima, S.1    Shimada, K.2    Vermeglio, A.3    Nagashima, K.V.4
  • 23
    • 0346106078 scopus 로고    scopus 로고
    • HiPIP in Rubrivivax gelatinosus is firmly associated to the membrane in a conformation efficient for electron transfer towards the photosynthetic reaction centre
    • Lieutaud C, Nitschke W, Vermeglio A, Parot P, Schoepp-Cothenet B. 2003. HiPIP in Rubrivivax gelatinosus is firmly associated to the membrane in a conformation efficient for electron transfer towards the photosynthetic reaction centre. Biochim. Biophys. Acta 1557:83-90. http://dx .doi.org/10.1016/S0005-2728(02)00397-3.
    • (2003) Biochim. Biophys. Acta , vol.1557 , pp. 83-90
    • Lieutaud, C.1    Nitschke, W.2    Vermeglio, A.3    Parot, P.4    Schoepp-Cothenet, B.5
  • 24
    • 0001228592 scopus 로고
    • In Blankenship RE, Madigan MT, Bauer CE (ed), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, Netherlands.
    • Nitschke W, Dracheva SM. 1995. Reaction center associated cytochromes, p 775-805. In Blankenship RE, Madigan MT, Bauer CE (ed), Anoxygenic photosynthetic bacteria. Kluwer Academic Publishers, Dordrecht, Netherlands.
    • (1995) Reaction center associated cytochromes , pp. 775-805
    • Nitschke, W.1    Dracheva, S.M.2
  • 25
    • 84878594153 scopus 로고    scopus 로고
    • Iron and copper act synergistically to delay anaerobic growth in bacteria
    • Bird LJ, Coleman ML, Newman DK. 2013. Iron and copper act synergistically to delay anaerobic growth in bacteria. Appl. Environ. Microbiol. 79:3619-3627. http://dx.doi.org/10.1128/AEM.03944-12.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 3619-3627
    • Bird, L.J.1    Coleman, M.L.2    Newman, D.K.3
  • 26
    • 80455163132 scopus 로고    scopus 로고
    • Cobalt stress in Escherichia coli and Salmonella enterica: molecular bases for toxicity and resistance
    • Barras F, Fontecave M. 2011. Cobalt stress in Escherichia coli and Salmonella enterica: molecular bases for toxicity and resistance. Metallomics 3:1130-1134. http://dx.doi.org/10.1039/c1mt00099c.
    • (2011) Metallomics , vol.3 , pp. 1130-1134
    • Barras, F.1    Fontecave, M.2
  • 27
    • 80455163148 scopus 로고    scopus 로고
    • Mechanisms of nickel toxicity in microorganisms
    • Macomber L, Hausinger RP. 2011. Mechanisms of nickel toxicity in microorganisms. Metallomics 3:1153-1162. http://dx.doi.org/10.1039 /c1mt00063b.
    • (2011) Metallomics , vol.3 , pp. 1153-1162
    • Macomber, L.1    Hausinger, R.P.2
  • 28
    • 56749157545 scopus 로고    scopus 로고
    • Functional coupling between reaction centers and cytochrome bc1 complexes
    • In Hunter N, Daldal F, Thurnauer M, Beatty T (ed), The purple phototrophic bacteria. Springer, Dordrecht, Netherlands
    • Lavergne J, Vermeglio A, Joliot P. 2009. Functional coupling between reaction centers and cytochrome bc1 complexes. In Hunter N, Daldal F, Thurnauer M, Beatty T (ed), The purple phototrophic bacteria. Springer, Dordrecht, Netherlands.
    • (2009)
    • Lavergne, J.1    Vermeglio, A.2    Joliot, P.3
  • 29
    • 0033985228 scopus 로고    scopus 로고
    • Iron and oxidative stress in bacteria
    • Touati D. 2000. Iron and oxidative stress in bacteria. Arch. Biochem. Biophys. 373:1-6. http://dx.doi.org/10.1006/abbi.1999.1518.
    • (2000) Arch. Biochem. Biophys. , vol.373 , pp. 1-6
    • Touati, D.1
  • 30
    • 57849118474 scopus 로고    scopus 로고
    • Structure and function of cytochrome c2: reaction center complex from Rhodobacter sphaeroides
    • In Hunter N, Daldal F, Thurnauer M, Beatty T (ed), The purple phototrophic bacteria. Springer, Dordrecht, Netherlands
    • Axelrod H, Miyashita O, Okamura M. 2009. Structure and function of cytochrome c2: reaction center complex from Rhodobacter sphaeroides, p 323-336. In Hunter N, Daldal F, Thurnauer M, Beatty T (ed), The purple phototrophic bacteria. Springer, Dordrecht, Netherlands.
    • (2009) , pp. 323-336
    • Axelrod, H.1    Miyashita, O.2    Okamura, M.3
  • 31
    • 0028167744 scopus 로고
    • Interaction between cytochrome c2 and reaction centers from purple bacteria
    • Wang S, Li X, Williams JC, Allen JP, Mathis P. 1994. Interaction between cytochrome c2 and reaction centers from purple bacteria. Biochemistry 33:8306-8312. http://dx.doi.org/10.1021/bi00193a018.
    • (1994) Biochemistry , vol.33 , pp. 8306-8312
    • Wang, S.1    Li, X.2    Williams, J.C.3    Allen, J.P.4    Mathis, P.5
  • 32
    • 0025922846 scopus 로고
    • Reaction of cytochrome c2 with photosynthetic reaction centers from Rhodopseudomonas viridis
    • Knaff DB, Willie A, Long JE, Kriauciunas A, Durham B, Millett F. 1991. Reaction of cytochrome c2 with photosynthetic reaction centers from Rhodopseudomonas viridis. Biochemistry 30:1303-1310. http://dx.doi .org/10.1021/bi00219a021.
    • (1991) Biochemistry , vol.30 , pp. 1303-1310
    • Knaff, D.B.1    Willie, A.2    Long, J.E.3    Kriauciunas, A.4    Durham, B.5    Millett, F.6
  • 33
    • 78650239608 scopus 로고    scopus 로고
    • Regulation of the phototrophic iron oxidation (pio) genes in Rhodopseudomonas palustris TIE-1 is mediated by the global regulator, FixK
    • Bose A, Newman DK. 2011. Regulation of the phototrophic iron oxidation (pio) genes in Rhodopseudomonas palustris TIE-1 is mediated by the global regulator, FixK. Mol. Microbiol. 79:63-75. http://dx.doi.org/10 .1111/j.1365-2958.2010.07430.x.
    • (2011) Mol. Microbiol. , vol.79 , pp. 63-75
    • Bose, A.1    Newman, D.K.2
  • 34
    • 0025904874 scopus 로고
    • Electrochemical redox titration of cofactors in the reaction center from Rhodobacter sphaeroides
    • Moss DA, Leonhard M, Bauscher M, Mantele W. 1991. Electrochemical redox titration of cofactors in the reaction center from Rhodobacter sphaeroides. FEBS Lett. 283:33-36. http://dx.doi.org/10.1016/0014-5793(91) 80547-G.
    • (1991) FEBS Lett. , vol.283 , pp. 33-36
    • Moss, D.A.1    Leonhard, M.2    Bauscher, M.3    Mantele, W.4
  • 35
    • 0027991814 scopus 로고
    • A membrane-bound HIPIP type center in the thermohalophile Rhodothermus marinus
    • Pereira MM, Antunes AM, Nunes OC, Da Costa MS, Teixeira M. 1994. A membrane-bound HIPIP type center in the thermohalophile Rhodothermus marinus. FEBS Lett. 352:327-330. http://dx.doi.org/10.1016 /0014-5793(94)00985-6.
    • (1994) FEBS Lett. , vol.352 , pp. 327-330
    • Pereira, M.M.1    Antunes, A.M.2    Nunes, O.C.3    Da Costa, M.S.4    Teixeira, M.5
  • 36
    • 0033604850 scopus 로고    scopus 로고
    • Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: a novel multihemic cytochrome bc, a new complex III
    • Pereira MM, Carita JN, Teixeira M. 1999. Membrane-bound electron transfer chain of the thermohalophilic bacterium Rhodothermus marinus: a novel multihemic cytochrome bc, a new complex III. Biochemistry 38:1268-1275. http://dx.doi.org/10.1021/bi9818063.
    • (1999) Biochemistry , vol.38 , pp. 1268-1275
    • Pereira, M.M.1    Carita, J.N.2    Teixeira, M.3
  • 37
    • 0037056056 scopus 로고    scopus 로고
    • The bc(1) complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction. Is there a second bc(1) complex?
    • Brasseur G, Bruscella P, Bonnefoy V, Lemesle-Meunier D. 2002. The bc(1) complex of the iron-grown acidophilic chemolithotrophic bacterium Acidithiobacillus ferrooxidans functions in the reverse but not in the forward direction. Is there a second bc(1) complex? Biochim. Biophys. Acta 1555:37-43. http://dx.doi.org/10.1016/S0005-2728(02)00251-7.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 37-43
    • Brasseur, G.1    Bruscella, P.2    Bonnefoy, V.3    Lemesle-Meunier, D.4
  • 38
    • 19044374613 scopus 로고    scopus 로고
    • The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms
    • Bruscella P, Cassagnaud L, Ratouchniak J, Brasseur G, Lojou E, Amils R, Bonnefoy V. 2005. The HiPIP from the acidophilic Acidithiobacillus ferrooxidans is correctly processed and translocated in Escherichia coli, in spite of the periplasm pH difference between these two micro-organisms. Microbiology 151(Pt 5):1421-1431. http://dx.doi.org/10.1099/mic.0.27476-0.
    • (2005) Microbiology , vol.151 , Issue.PART 5 , pp. 1421-1431
    • Bruscella, P.1    Cassagnaud, L.2    Ratouchniak, J.3    Brasseur, G.4    Lojou, E.5    Amils, R.6    Bonnefoy, V.7
  • 39
    • 0033120863 scopus 로고    scopus 로고
    • Fe-S proteins in sensing and regulatory functions
    • Beinert H, Kiley PJ. 1999. Fe-S proteins in sensing and regulatory functions. Curr. Opin. Chem. Biol. 3:152-157. http://dx.doi.org/10.1016 /S1367-5931(99)80027-1.
    • (1999) Curr. Opin. Chem. Biol , vol.3 , pp. 152-157
    • Beinert, H.1    Kiley, P.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.