메뉴 건너뛰기




Volumn 34, Issue , 1999, Pages 85-100

Oxygen-carrying proteins: Three solutions to a common problem

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; HEMERYTHRIN; HEMOCYANIN; HEMOGLOBIN; METAL; OXYGEN;

EID: 0033289110     PISSN: 00711365     EISSN: None     Source Type: Journal    
DOI: 10.1042/bse0340085     Document Type: Article
Times cited : (40)

References (30)
  • 2
    • 33847798770 scopus 로고
    • Dioxygen-metal complexes: Toward a unified view
    • Vaska, L. (1976) Dioxygen-metal complexes: toward a unified view. Acc. Chem. Res. 9, 175-183
    • (1976) Acc. Chem. Res. , vol.9 , pp. 175-183
    • Vaska, L.1
  • 3
    • 85009192854 scopus 로고
    • Metal-dioxygen complexes
    • Klotz, I.M. & Kurtz, Jr., D.M. (eds.) (1994) Metal-dioxygen complexes. Chem. Rev. 94, 567-856
    • (1994) Chem. Rev. , vol.94 , pp. 567-856
    • Klotz, I.M.1    Kurtz Jr., D.M.2
  • 5
    • 0019209443 scopus 로고
    • Structure and refinement of oxymyoglobin at 1.6 Å resolution
    • Phillips, S.E.V. (1980) Structure and refinement of oxymyoglobin at 1.6 Å resolution. J. Mol. Biol. 142, 531-554
    • (1980) J. Mol. Biol. , vol.142 , pp. 531-554
    • Phillips, S.E.V.1
  • 6
    • 0021027685 scopus 로고
    • Structure of human oxyhaemoglobin at 2.1 Å resolution
    • Shaanan, B. (1983) Structure of human oxyhaemoglobin at 2.1 Å resolution. J. Mol. Biol. 171, 31-59
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 7
    • 0000043761 scopus 로고
    • Dioxygen and hemerythrin
    • Stenkamp, R.E. (1994) Dioxygen and hemerythrin. Chem. Rev. 94, 715-726
    • (1994) Chem. Rev. , vol.94 , pp. 715-726
    • Stenkamp, R.E.1
  • 8
    • 0027981519 scopus 로고
    • Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
    • Magnus, K.A., Hazes, B., Tonthat, H., Bonaventura, C., Bonaventura, J. & Hol, W.G.J. (1994) Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences. Proteins Struct. Funct Genet. 19, 302-309
    • (1994) Proteins Struct. Funct Genet. , vol.19 , pp. 302-309
    • Magnus, K.A.1    Hazes, B.2    Tonthat, H.3    Bonaventura, C.4    Bonaventura, J.5    Hol, W.G.J.6
  • 9
    • 0000200878 scopus 로고
    • Recent structural work on the oxygen transport protein hemocyanin
    • Magnus, K.A., Ton-That, H. & Carpenter, J.E. (1994) Recent structural work on the oxygen transport protein hemocyanin. Chem. Rev. 94, 727-735
    • (1994) Chem. Rev. , vol.94 , pp. 727-735
    • Magnus, K.A.1    Ton-That, H.2    Carpenter, J.E.3
  • 10
    • 0000094068 scopus 로고
    • The magnetic properties and structure of hemoglobin, oxyhemoglobin and carbonmonoxyhemoglobin
    • Pauling, L. & Coryell, C.D. (1936) The magnetic properties and structure of hemoglobin, oxyhemoglobin and carbonmonoxyhemoglobin. Proc. Natl. Acad. Sci. U.S.A. 22, 210-216
    • (1936) Proc. Natl. Acad. Sci. U.S.A. , vol.22 , pp. 210-216
    • Pauling, L.1    Coryell, C.D.2
  • 11
    • 3042907629 scopus 로고
    • Synthetic heme dioxygen complexes
    • Momenteau, M. & Reed, C.A. (1994) Synthetic heme dioxygen complexes. Chem. Rev. 94, 659-698
    • (1994) Chem. Rev. , vol.94 , pp. 659-698
    • Momenteau, M.1    Reed, C.A.2
  • 12
    • 0001568219 scopus 로고
    • Theoretical calculations of metal-dioxygen complexes
    • Bytheway, I. & Hall, M.B. (1994) Theoretical calculations of metal-dioxygen complexes. Chem. Rev. 94, 639-658
    • (1994) Chem. Rev. , vol.94 , pp. 639-658
    • Bytheway, I.1    Hall, M.B.2
  • 14
    • 0030876309 scopus 로고    scopus 로고
    • Myoglobin and CO: Structure, energetics, and disorder
    • Sage, J.T. (1997) Myoglobin and CO: structure, energetics, and disorder. J. Biol. Inorg. Chem. 2, 537-543
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 537-543
    • Sage, J.T.1
  • 15
    • 0030882198 scopus 로고    scopus 로고
    • Modulating carbon monoxide binding affinity and kinetics in myoglobin: The roles of the distal histidine and the heme pocket docking site
    • Lim, M., Jackson, T.A. & Anfinrud, P.A. (1997) Modulating carbon monoxide binding affinity and kinetics in myoglobin: the roles of the distal histidine and the heme pocket docking site. J. Biol. Inorg. Chem. 2, 531-536
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 531-536
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 16
    • 0001197916 scopus 로고
    • Binuclear Iron Proteins
    • Loehr, T.M., ed., VCR, New York
    • Sanders-Loehr, J. (1989) Binuclear Iron Proteins. In Iron Carriers and Iron Proteins (Loehr, T.M., ed.), pp. 373-466, VCR, New York
    • (1989) Iron Carriers and Iron Proteins , pp. 373-466
    • Sanders-Loehr, J.1
  • 18
    • 0009411657 scopus 로고
    • Reactions of non-heme iron(II) centers with dioxygen in biology and chemistry
    • Feig, A.L. & Lippard, S.J. (1994) Reactions of non-heme iron(II) centers with dioxygen in biology and chemistry. Chem. Rev. 94, 759-805
    • (1994) Chem. Rev. , vol.94 , pp. 759-805
    • Feig, A.L.1    Lippard, S.J.2
  • 20
    • 33751156088 scopus 로고
    • Formation and deoxygenation kinetics of oxyhemerythrin and oxyhemocyanin. A pressure dependence study
    • Projahn, H.-D., Schindler, S., van Eldik, R., Fortier, D.G., Andrew, C.R. & Sykes, A.G. (1995) Formation and deoxygenation kinetics of oxyhemerythrin and oxyhemocyanin. A pressure dependence study. Inorg. Chem. 34, 5935-5941
    • (1995) Inorg. Chem. , vol.34 , pp. 5935-5941
    • Projahn, H.-D.1    Schindler, S.2    Van Eldik, R.3    Fortier, D.G.4    Andrew, C.R.5    Sykes, A.G.6
  • 21
    • 0029638226 scopus 로고
    • 2 by myohemerythrin. Evidence for different rate-determining steps and a caveat
    • 2 by myohemerythrin. Evidence for different rate-determining steps and a caveat. J. Am. Chem. Soc. 117, 11993-11994
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11993-11994
    • Lloyd, C.R.1    Eyring, E.M.2    Ellis Jr., W.E.3
  • 22
    • 0030921451 scopus 로고    scopus 로고
    • Functional role of leucine-103 in myohemerythrin
    • Raner, G.M., Martins, L.J. & Ellis, Jr., W.R. (1997) Functional role of leucine-103 in myohemerythrin. Biochemistry 36, 7037-7043
    • (1997) Biochemistry , vol.36 , pp. 7037-7043
    • Raner, G.M.1    Martins, L.J.2    Ellis Jr., W.R.3
  • 24
    • 0001084385 scopus 로고
    • Copper-dioxygen complexes. Inorganic and bioinorganic perspectives
    • Kitajima, N. & Moro-oka, Y. (1994) Copper-dioxygen complexes. Inorganic and bioinorganic perspectives. Chem. Rev. 94, 737-767
    • (1994) Chem. Rev. , vol.94 , pp. 737-767
    • Kitajima, N.1    Moro-oka, Y.2
  • 25
  • 26
    • 0030815015 scopus 로고    scopus 로고
    • Evidence for a cysteine-histidine thioether bridge in functional molluscan haemocyanins and location of the disulfide bridges in functional units d and g of the betaC-haemocyanin of Helix pomatia
    • Gielens, C., De Geest, N., Xin, X.Q., Devreese, B., Van Beeumen, J. & Preaux, G. (1997) Evidence for a cysteine-histidine thioether bridge in functional molluscan haemocyanins and location of the disulfide bridges in functional units d and g of the betaC-haemocyanin of Helix pomatia. Eur. J. Biochem. 248, 879-888
    • (1997) Eur. J. Biochem. , vol.248 , pp. 879-888
    • Gielens, C.1    De Geest, N.2    Xin, X.Q.3    Devreese, B.4    Van Beeumen, J.5    Preaux, G.6
  • 27
    • 12644273812 scopus 로고    scopus 로고
    • Structural similarity and functional diversity in diiron-oxo proteins
    • Kurtz, Jr., D.M. (1997) Structural similarity and functional diversity in diiron-oxo proteins. J. Biol. Inorg. Chem. 2, 159-167
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 159-167
    • Kurtz Jr., D.M.1
  • 30
    • 0000239991 scopus 로고    scopus 로고
    • Dioxyen activation by enzymes containing binuclear non-heme iron clusters
    • Waller, B.J. & Lipscomb, J.D. (1996) Dioxyen activation by enzymes containing binuclear non-heme iron clusters. Chem. Rev. 96, 2625-2657
    • (1996) Chem. Rev. , vol.96 , pp. 2625-2657
    • Waller, B.J.1    Lipscomb, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.