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Volumn 7, Issue 12, 1999, Pages

Still a puzzle: Why is haem covalently attached in c-type cytochromes?

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME; CYTOCHROME C; PROTOPORPHYRIN;

EID: 0033573140     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)88334-3     Document Type: Review
Times cited : (148)

References (61)
  • 3
    • 0021101958 scopus 로고
    • Why do c-type cytochromes exist?
    • 3. Wood, P.M. (1983). Why do c-type cytochromes exist? FEBS Lett. 164, 223-226.
    • (1983) FEBS Lett. , vol.164 , pp. 223-226
    • Wood, P.M.1
  • 4
    • 0025905797 scopus 로고
    • Why do c-type cytochromes exist? Reprise
    • 4. Wood, P.M. (1991). Why do c-type cytochromes exist? Reprise. Biochim. Biophys. Acta 1058, 5-7.
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 5-7
    • Wood, P.M.1
  • 5
    • 0032031987 scopus 로고    scopus 로고
    • Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplasts and bacteria
    • 5. Page, M.D., Sambongi, Y. & Ferguson, S.J. (1998). Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplasts and bacteria Trends Biochem. Sci. 23, 103-108.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 103-108
    • Page, M.D.1    Sambongi, Y.2    Ferguson, S.J.3
  • 6
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • 6. Kranz, R., Lill, R., Goldman, B., Bonnard, G. & Merchant, S. (1998). Molecular mechanisms of cytochrome c biogenesis: three distinct systems. Mol. Microbiol. 29, 383-396.
    • (1998) Mol. Microbiol. , vol.29 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 7
    • 0009058518 scopus 로고
    • Mechanism of a novel synthesis of haemin c from protohaemin and L-cysteine. A Markownikoff-type radical addition reaction
    • 7. Kojo, S. & Sano, S. (1981). Mechanism of a novel synthesis of haemin c from protohaemin and L-cysteine. A Markownikoff-type radical addition reaction. J. Chem. Soc., 2864-2870.
    • (1981) J. Chem. Soc. , pp. 2864-2870
    • Kojo, S.1    Sano, S.2
  • 8
    • 0032555539 scopus 로고    scopus 로고
    • Prototype of a heme chaperone essential for cytochrome c maturation
    • 8. Schulz, H., Hennecke, H. & Thony-Meyer, L. (1998). Prototype of a heme chaperone essential for cytochrome c maturation. Science 281, 1197-1200.
    • (1998) Science , vol.281 , pp. 1197-1200
    • Schulz, H.1    Hennecke, H.2    Thony-Meyer, L.3
  • 9
    • 0032529951 scopus 로고    scopus 로고
    • The CcmE protein from Escherichia coli is a haem-binding protein
    • 9. Reid, E., Eaves, D.J. & Cole, J.A. (1998). The CcmE protein from Escherichia coli is a haem-binding protein. FEMS Microbiol. Lett. 166, 369-375.
    • (1998) FEMS Microbiol. Lett. , vol.166 , pp. 369-375
    • Reid, E.1    Eaves, D.J.2    Cole, J.A.3
  • 10
    • 0027280029 scopus 로고
    • Transmutation of a heme protein
    • 10. Barker, P.D., et al., & Mauk, A.G. (1993). Transmutation of a heme protein. Proc. Natl Acad. Sci. USA 90, 6542-6546.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 6542-6546
    • Barker, P.D.1    Mauk, A.G.2
  • 12
    • 0032524917 scopus 로고    scopus 로고
    • 552 gene from Thermus thermophilus HB8 - Evidence for genetic linkage to an ATP-binding cassette protein and initial characterization of the cycA gene products
    • 552 gene from Thermus thermophilus HB8 - evidence for genetic linkage to an ATP-binding cassette protein and initial characterization of the cycA gene products. J. Biol. Chem. 273, 12006-12016.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12006-12016
    • Keightley, J.A.1    Sanders, D.2    Todaro, T.R.3    Pastuszyn, A.4    Fee, J.A.5
  • 13
    • 0032539517 scopus 로고    scopus 로고
    • A stable, molten-globule-like cytochrome c
    • 13. Wittung-Stafshede, P. (1998). A stable, molten-globule-like cytochrome c. Biochim. Biophys. Acta 1382, 324-332.
    • (1998) Biochim. Biophys. Acta , vol.1382 , pp. 324-332
    • Wittung-Stafshede, P.1
  • 14
    • 0024408905 scopus 로고
    • Import of cytochrome c into mitochondria: Reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c
    • 14. Nicholson, D.W. & Neupert, W. (1989). Import of cytochrome c into mitochondria: reduction of heme, mediated by NADH and flavin nucleotides, is obligatory for its covalent linkage to apocytochrome c. Proc. Natl Acad. Sci. USA 86, 4340-4344.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4340-4344
    • Nicholson, D.W.1    Neupert, W.2
  • 15
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • 15. Pollock, W.B.R., Rosell, F.I., Twitchett, M.B., Dumont, M.E. & Mauk, A.G. (1998). Bacterial expression of a mitochondrial cytochrome c. Trimethylation of Lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry 37, 6124-6131.
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.R.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 16
    • 0032583439 scopus 로고    scopus 로고
    • Effects of ligation and folding on reduction potentials of heme proteins
    • 16. Tezcan, F.A., Winkler, J.R. & Gray, H.B. (1998). Effects of ligation and folding on reduction potentials of heme proteins. J. Am. Chem. Soc. 120, 13383-13388.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13383-13388
    • Tezcan, F.A.1    Winkler, J.R.2    Gray, H.B.3
  • 17
    • 0028773015 scopus 로고
    • Crystal-structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • 17. Martinez, S.E., Huang, D., Szczepaniak, A., Cramer, W.A. & Smith, J.L. (1994). Crystal-structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 2, 95-105.
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, D.2    Szczepaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 19
    • 0032979703 scopus 로고    scopus 로고
    • The crystal structure of HasA, a hemophore secreted by Serratia marcescens
    • 19. Arnoux, P., et al., & Czjzek, M. (1999). The crystal structure of HasA, a hemophore secreted by Serratia marcescens. Nat. Struct. Biol. 6, 516-520.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 516-520
    • Arnoux, P.1    Czjzek, M.2
  • 20
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains
    • 20. Paoli, M., Anderson, B.F., Baker, H.M., Morgan, W.T., Smith, A. & Baker, E.N. (1999). Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two β-propeller domains. Nat. Struct. Biol. 6, 926-931.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 21
    • 0033573859 scopus 로고    scopus 로고
    • A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability properties
    • 21. Thorsteinsson, M.V., et al., & Olson, J.A. (1999). A cyanobacterial hemoglobin with unusual ligand binding kinetics and stability properties. Biochemistry 38, 2117-2126.
    • (1999) Biochemistry , vol.38 , pp. 2117-2126
    • Thorsteinsson, M.V.1    Olson, J.A.2
  • 25
    • 0030611275 scopus 로고    scopus 로고
    • The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea
    • 25 Igarashi, N., Moriyama, H., Fujiwara, T., Fukumori, Y. & Tanaka, N. (1997). The 2.8 Å structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea. Nat. Struct. Biol. 4, 276-284.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 276-284
    • Igarashi, N.1    Moriyama, H.2    Fujiwara, T.3    Fukumori, Y.4    Tanaka, N.5
  • 27
    • 0033615050 scopus 로고    scopus 로고
    • Structure of cytochrome c nitrite reductase
    • 27. Einsle, O., et al., & Kroneck, P.M.H. (1999). Structure of cytochrome c nitrite reductase. Nature 400, 476-480.
    • (1999) Nature , vol.400 , pp. 476-480
    • Einsle, O.1    Kroneck, P.M.H.2
  • 28
    • 0031895861 scopus 로고    scopus 로고
    • 552 nitrite reductase from Escherichia coli
    • 552 nitrite reductase from Escherichia coli. Mol. Microbiol. 28, 205-216.
    • (1998) Mol. Microbiol. , vol.28 , pp. 205-216
    • Eaves, D.J.1    Cole, J.A.2
  • 29
    • 0030773395 scopus 로고    scopus 로고
    • A preliminary analysis of the three-dimensional structure of dimeric dihaem split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774 at 2.5 Å resolution using the MAD phasing method: A novel cytochrome fold with a stacked-haem arrangement
    • 29. Matias, P.M., et al., & Carrondo, M. A. (1997). A preliminary analysis of the three-dimensional structure of dimeric dihaem split-Soret cytochrome c from Desulfovibrio desulfuricans ATCC 27774 at 2.5 Å resolution using the MAD phasing method: a novel cytochrome fold with a stacked-haem arrangement. J. Biol. Inorg. Chem. 2, 507-514.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 507-514
    • Matias, P.M.1    Carrondo, M.A.2
  • 30
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • 30. Murzin, A.G., Brenner, S.E., Hubbard, T. & Chothia, C. (1995). SCOP: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 31
    • 0022419653 scopus 로고
    • Structure of ferricytochrome ć from Rhodospirillum molischianum at 1.67 Å resolution
    • 31. Finzel, B.C., Weber, P.C., Hardman, K.D. & Salemme, F.R. (1985). Structure of ferricytochrome ć from Rhodospirillum molischianum at 1.67 Å resolution. J. Mol. Biol. 186, 627-643.
    • (1985) J. Mol. Biol. , vol.186 , pp. 627-643
    • Finzel, B.C.1    Weber, P.C.2    Hardman, K.D.3    Salemme, F.R.4
  • 32
    • 0032507002 scopus 로고    scopus 로고
    • Co- and counterrotation of magnetic axes and axial ligands in low-spin ferriheme systems
    • 32. Shokhirev, N.V. & Walker, F.A. (1998). Co-and counterrotation of magnetic axes and axial ligands in low-spin ferriheme systems. J. Am. Chem. Soc. 120, 981-990.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 981-990
    • Shokhirev, N.V.1    Walker, F.A.2
  • 35
    • 0031904598 scopus 로고    scopus 로고
    • Conservation of the conformation of the porphyrin macrocycle in hemoproteins
    • 35. Jentzen, W., Ma, J.-G. & Shelnutt, J.A. (1998). Conservation of the conformation of the porphyrin macrocycle in hemoproteins. Biophys. J. 74, 753-763.
    • (1998) Biophys. J. , vol.74 , pp. 753-763
    • Jentzen, W.1    Ma, J.-G.2    Shelnutt, J.A.3
  • 38
    • 0000693098 scopus 로고
    • Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins
    • 38. La Mar, G.N., Budd, D.L., Viscio, D.B., Smith, K.M. & Langry, K.C. (1978). Proton nuclear magnetic resonance characterization of heme disorder in hemoproteins. Proc. Natl Acad. Sci. USA 75, 5755-5759.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 5755-5759
    • La Mar, G.N.1    Budd, D.L.2    Viscio, D.B.3    Smith, K.M.4    Langry, K.C.5
  • 39
    • 0021112460 scopus 로고
    • Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein
    • 39. La Mar, G.N., Davis, N.L., Parish, D.W. & Smith, K.M. (1983). Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein. J. Mol. Biol. 168, 887-896.
    • (1983) J. Mol. Biol. , vol.168 , pp. 887-896
    • La Mar, G.N.1    Davis, N.L.2    Parish, D.W.3    Smith, K.M.4
  • 40
    • 0025315531 scopus 로고
    • Site-directedly mutated human cytochrome c which retains heme c via only one thioether bond
    • 40. Tanaka, Y., Kubota, I., Amachi, T., Yoshizumi, H. & Matsubara, H. (1990). Site-directedly mutated human cytochrome c which retains heme c via only one thioether bond. J. Biochem. 108, 7-8.
    • (1990) J. Biochem. , vol.108 , pp. 7-8
    • Tanaka, Y.1    Kubota, I.2    Amachi, T.3    Yoshizumi, H.4    Matsubara, H.5
  • 41
    • 0023677342 scopus 로고
    • The binding characteristics of the cytochrome c iron
    • 41. Schejter, A. & Plotkin, B. (1988). The binding characteristics of the cytochrome c iron. Biochem. J. 255, 353-356.
    • (1988) Biochem. J. , vol.255 , pp. 353-356
    • Schejter, A.1    Plotkin, B.2
  • 42
    • 0025981785 scopus 로고
    • The reactivity of cytochrome c with soft ligands
    • 42. Schejter, A., Plotkin, B. & Vig, I. (1991). The reactivity of cytochrome c with soft ligands. FEBS Lett. 280, 199-201.
    • (1991) FEBS Lett. , vol.280 , pp. 199-201
    • Schejter, A.1    Plotkin, B.2    Vig, I.3
  • 43
    • 0542421561 scopus 로고    scopus 로고
    • Kinetic and structural analysis of submillisecond folding events in cytochrome c
    • 43. Shastry, M.C.R., Sander, J.M. & Roder, H. (1998). Kinetic and structural analysis of submillisecond folding events in cytochrome c. Acc. Chem. Res. 31, 717-725.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 717-725
    • Shastry, M.C.R.1    Sander, J.M.2    Roder, H.3
  • 44
    • 0000519105 scopus 로고    scopus 로고
    • Cytochrome c folding and unfolding: A biphasic mechanism
    • 44. Yeh, S.-R., Han, S.W. & Rousseau, D.L (1998). Cytochrome c folding and unfolding: a biphasic mechanism Acc. Chem. Res. 31, 727-736.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 727-736
    • Yeh, S.-R.1    Han, S.W.2    Rousseau, D.L.3
  • 46
    • 0015524145 scopus 로고
    • The conformation of horse heart apocytochrome c
    • 46. Stellwagen, E., Rysavy, R. & Babul, G. (1972). The conformation of horse heart apocytochrome c. J. Biol. Chem. 247, 8074-8077.
    • (1972) J. Biol. Chem. , vol.247 , pp. 8074-8077
    • Stellwagen, E.1    Rysavy, R.2    Babul, G.3
  • 47
    • 0015951392 scopus 로고
    • Spectroscopic studies on the conformation of cytochrome c and apocytochrome c
    • 47. Cohen, J.S., Fisher, W.R. & Schechter, A.N. (1974). Spectroscopic studies on the conformation of cytochrome c and apocytochrome c. J. Biol. Chem. 249, 1113-1118.
    • (1974) J. Biol. Chem. , vol.249 , pp. 1113-1118
    • Cohen, J.S.1    Fisher, W.R.2    Schechter, A.N.3
  • 48
    • 0028244331 scopus 로고
    • Noncovalent binding of heme induces a compact apocytochrome c structure
    • 48. Dumont, M.E., Corin, A.F. & Campbell, G.A. (1994). Noncovalent binding of heme induces a compact apocytochrome c structure. Biochemistry 33, 7368-7378.
    • (1994) Biochemistry , vol.33 , pp. 7368-7378
    • Dumont, M.E.1    Corin, A.F.2    Campbell, G.A.3
  • 51
    • 1842412487 scopus 로고    scopus 로고
    • Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme
    • 51. Williams, P.A., Fulop, V., Garman, E.F., Saunders, N.F., Ferguson, S.J. & Hajdu, J. (1997). Haem-ligand switching during catalysis in crystals of a nitrogen-cycle enzyme Nature 389, 406-412.
    • (1997) Nature , vol.389 , pp. 406-412
    • Williams, P.A.1    Fulop, V.2    Garman, E.F.3    Saunders, N.F.4    Ferguson, S.J.5    Hajdu, J.6
  • 52
    • 0028853285 scopus 로고
    • Structure of the green heme in myeloperoxidase
    • 52. Fenna, R., Zeng, J. & Davey, C. (1995). Structure of the green heme in myeloperoxidase. Arch. Biochem. Biophys. 316, 653-656.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 653-656
    • Fenna, R.1    Zeng, J.2    Davey, C.3
  • 53
    • 0030910381 scopus 로고    scopus 로고
    • Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group
    • 53. DePillis, G.D., Ozaki, S., Kuo, J.M., Maltby, D.A. & Ortiz de Montellano, P.R. (1997). Autocatalytic processing of heme by lactoperoxidase produces the native protein-bound prosthetic group. J. Biol. Chem. 272, 8857-8860.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8857-8860
    • DePillis, G.D.1    Ozaki, S.2    Kuo, J.M.3    Maltby, D.A.4    Ortiz De Montellano, P.R.5
  • 54
    • 0033609516 scopus 로고    scopus 로고
    • Structure of the soluble domain of cytochrome f from the cyanobacterium Phornidium laminosum
    • 54. Carrell, C.J., Schlarb, B.G., Bendall, D.S., Howe, C.J., Cramer, W.A. & Smith, J.L. (1999). Structure of the soluble domain of cytochrome f from the cyanobacterium Phornidium laminosum. Biochemistry 38, 9590-9599.
    • (1999) Biochemistry , vol.38 , pp. 9590-9599
    • Carrell, C.J.1    Schlarb, B.G.2    Bendall, D.S.3    Howe, C.J.4    Cramer, W.A.5    Smith, J.L.6
  • 55
    • 0032582701 scopus 로고    scopus 로고
    • Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport
    • 55. Roldan, M.D., et al., & Richardson, D.J. (1998). Spectroscopic characterization of a novel multiheme c-type cytochrome widely implicated in bacterial electron transport. J. Biol. Chem. 273, 28785-28790.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28785-28790
    • Roldan, M.D.1    Richardson, D.J.2
  • 56
    • 0030903069 scopus 로고    scopus 로고
    • Outer membrane cytochromes of Shewanella putrefaciens MR-1 : Spectral analysis, and purification of the 83 kDa c-type cytochrome
    • 56. Myers, C.R. & Myers, J.M. (1997). Outer membrane cytochromes of Shewanella putrefaciens MR-1 : spectral analysis, and purification of the 83 kDa c-type cytochrome. Biochim. Biophys. Acta 1326, 307-318.
    • (1997) Biochim. Biophys. Acta , vol.1326 , pp. 307-318
    • Myers, C.R.1    Myers, J.M.2
  • 57
    • 0026011830 scopus 로고
    • 1 -dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins
    • 1 -dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme proteins. FEBS Lett. 279, 205-209.
    • (1991) FEBS Lett. , vol.279 , pp. 205-209
    • Jungst, A.1    Wakabayashi, S.2    Matsubara, H.3    Zumft, W.G.4
  • 58
    • 0029645915 scopus 로고
    • Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa
    • 58. Fulop, V., Ridout, C.J., Greenwood, C. & Hajdu, J. (1995). Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa. Structure 3, 1225-1233.
    • (1995) Structure , vol.3 , pp. 1225-1233
    • Fulop, V.1    Ridout, C.J.2    Greenwood, C.3    Hajdu, J.4
  • 59
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • 59. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 60
    • 0000732609 scopus 로고
    • GRASP - Graphical representation and analysis of surface properties
    • 60. Nicholls, A., Bharadwaj, R. & Honig, B. (1993). GRASP - graphical representation and analysis of surface properties. Biophys. J. 64, A166.
    • (1993) Biophys. J. , vol.64
    • Nicholls, A.1    Bharadwaj, R.2    Honig, B.3
  • 61
    • 0030815133 scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • 61. Merritt, E.A. & Bacon, D.J. (1977). Raster3D: photorealistic molecular graphics. Methods Enzymol. 277, 505-524.
    • (1977) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


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