메뉴 건너뛰기




Volumn 38, Issue 12, 2005, Pages 943-954

Metalloporphyrin - NO bonding: Building bridges with organometallic chemistry

Author keywords

[No Author keywords available]

Indexed keywords

HEMOPROTEIN; METALLOPORPHYRIN; NITRIC OXIDE; ORGANOMETALLIC COMPOUND;

EID: 30944431884     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar050121+     Document Type: Article
Times cited : (102)

References (52)
  • 1
    • 0030773396 scopus 로고    scopus 로고
    • 2, NO, and CO by electrostatic interactions with the bound ligand
    • 2, NO, and CO by electrostatic interactions with the bound ligand. J. Biol. Inorg. Chem. 1997, 2, 544-552.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 544-552
    • Olson, J.S.1    Phillips, G.N.2
  • 2
    • 16244376841 scopus 로고    scopus 로고
    • Ligand specificity of H-NOX domains: From sGC to bacterial NO sensors
    • Boon, E. M.; Marletta, M. A. Ligand specificity of H-NOX domains: From sGC to bacterial NO sensors. J. Inorg. Biochem. 2005, 99, 892-902.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 892-902
    • Boon, E.M.1    Marletta, M.A.2
  • 3
    • 33748590497 scopus 로고    scopus 로고
    • Carbonyl tilting and bending potential energy surface of carbon monoxyhemes
    • Ghosh, A.; Bocian, D. F. Carbonyl tilting and bending potential energy surface of carbon monoxyhemes. J. Phys. Chem. 1996, 100, 6363-6367.
    • (1996) J. Phys. Chem. , vol.100 , pp. 6363-6367
    • Ghosh, A.1    Bocian, D.F.2
  • 4
    • 0035110522 scopus 로고    scopus 로고
    • Is the CO adduct of myoglobin bent, and does it matter?
    • Spiro, T. G.; Kozlowski, P. M. Is the CO adduct of myoglobin bent, and does it matter? Acc. Chem. Res. 2001, 34, 137-144.
    • (2001) Acc. Chem. Res. , vol.34 , pp. 137-144
    • Spiro, T.G.1    Kozlowski, P.M.2
  • 6
    • 33847089519 scopus 로고
    • Qualitative discussion of alternative coordination modes of diatomic ligands in transition-metal complexes
    • Hoffmann, R.; Chen, M. M. L.; Thorn, D. L. Qualitative discussion of alternative coordination modes of diatomic ligands in transition-metal complexes. Inorg. Chem. 1977, 16, 503-511.
    • (1977) Inorg. Chem. , vol.16 , pp. 503-511
    • Hoffmann, R.1    Chen, M.M.L.2    Thorn, D.L.3
  • 8
    • 0000095969 scopus 로고
    • Deformability of heme protein CO adducts - FT-IR assignment of the FeCO bending mode
    • Hu, S. Z.; Vogel, K. M.; Spiro, T. G. Deformability of heme protein CO adducts - FT-IR assignment of the FeCO bending mode. J. Am. Chem. Soc. 1994, 116, 11187-11188.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11187-11188
    • Hu, S.Z.1    Vogel, K.M.2    Spiro, T.G.3
  • 9
    • 0029647452 scopus 로고
    • Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O
    • Lim, M.; Jackson, T. A.; Anfinrud, P. A. Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O. Science 1995, 269, 962-966.
    • (1995) Science , vol.269 , pp. 962-966
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 10
    • 0001397162 scopus 로고    scopus 로고
    • Discordant results on FeCO deformability in heme proteins reconciled by density functional theory
    • Spiro, T. G.; Kozlowski, P. M. Discordant results on FeCO deformability in heme proteins reconciled by density functional theory. J. Am. Chem. Soc. 1998, 120, 4524-4525.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 4524-4525
    • Spiro, T.G.1    Kozlowski, P.M.2
  • 11
    • 0032495930 scopus 로고    scopus 로고
    • Can the FeCO bending be higher than the FeC stretching frequency in CO adducts of heme proteins?
    • Papai, I.; Stirling, A.; Mink, J.; Nakamoto, K. Can the FeCO bending be higher than the FeC stretching frequency in CO adducts of heme proteins? Chem. Phys. Lett. 1998, 287, 531-534.
    • (1998) Chem. Phys. Lett. , vol.287 , pp. 531-534
    • Papai, I.1    Stirling, A.2    Mink, J.3    Nakamoto, K.4
  • 13
    • 0034679050 scopus 로고    scopus 로고
    • Intrinsic structural distortions in five-coordinate (nitrosyl)iron(II) porphyrinate derivatives
    • Scheidt, W. R.; Duval, H. F.; Neal, T. J.; Ellison, M. K. Intrinsic structural distortions in five-coordinate (nitrosyl)iron(II) porphyrinate derivatives. J. Am. Chem. Soc. 2000, 122, 4651-4659.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 4651-4659
    • Scheidt, W.R.1    Duval, H.F.2    Neal, T.J.3    Ellison, M.K.4
  • 14
    • 0034706052 scopus 로고    scopus 로고
    • A theoretical study of axial tilting and equatorial asymmetry in metalloporphyrin-nitrosyl com-plexes
    • Ghosh, A.; Wondimagegn, T. A theoretical study of axial tilting and equatorial asymmetry in metalloporphyrin-nitrosyl com-plexes. J. Am. Chem. Soc. 2000, 122, 8101-8102.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8101-8102
    • Ghosh, A.1    Wondimagegn, T.2
  • 15
    • 27744500686 scopus 로고    scopus 로고
    • Toward modeling H-NOX domains: A DFT study of heme-NO complexes as hydrogen bond acceptors
    • Tangen, E.; Svadberg, A.; Ghosh, A. Toward modeling H-NOX domains: A DFT study of heme-NO complexes as hydrogen bond acceptors. Inorg. Chem. 2005, 44, 7802-7805.
    • (2005) Inorg. Chem. , vol.44 , pp. 7802-7805
    • Tangen, E.1    Svadberg, A.2    Ghosh, A.3
  • 16
    • 0031276121 scopus 로고    scopus 로고
    • Equilibrium geometries and electronic structure of iron-porphyrin complexes: A density functional study
    • Rovira, C.; Kunc, K.; Hutter, J.; Ballone, P.; Parrinello, M. Equilibrium geometries and electronic structure of iron-porphyrin complexes: A density functional study. J. Phys. Chem. A 1997, 101, 8914-8925.
    • (1997) J. Phys. Chem. A , vol.101 , pp. 8914-8925
    • Rovira, C.1    Kunc, K.2    Hutter, J.3    Ballone, P.4    Parrinello, M.5
  • 17
    • 28844482457 scopus 로고    scopus 로고
    • Structural origin of two paramagnetic species in six-coordinated nitrosoiron(II) porphyrins revealed by Density Functional Theory analysis of the g tensors
    • Patchkovskii, S.; Ziegler, T. Structural origin of two paramagnetic species in six-coordinated nitrosoiron(II) porphyrins revealed by Density Functional Theory analysis of the g tensors. J. Phys. Chem. A 1997, 101, 8914-8925.
    • (1997) J. Phys. Chem. A , vol.101 , pp. 8914-8925
    • Patchkovskii, S.1    Ziegler, T.2
  • 18
    • 30944467758 scopus 로고    scopus 로고
    • note
    • From this point onward, all calculated results refer to DFT calculations using the PW91 exchange-correlation functional and Slater-type triple-ζ plus polarization basis sets, as implemented in the ADF program system.
  • 19
    • 0001417782 scopus 로고
    • Nitric oxide-triggered heme-mediated hydrolysis - A possible model for biological reactions of NO
    • Traylor, T. G.; Duprat, A. F.; Sharma, V. S. Nitric oxide-triggered heme-mediated hydrolysis - A possible model for biological reactions of NO. J. Am. Chem. Soc. 1993, 115, 810-811.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 810-811
    • Traylor, T.G.1    Duprat, A.F.2    Sharma, V.S.3
  • 20
    • 0033579189 scopus 로고    scopus 로고
    • NO disproportionation reactivity of Fe tropocoronand complexes
    • Franz, K. J.; Lippard, S. J. NO disproportionation reactivity of Fe tropocoronand complexes. J. Am. Chem. Soc. 1999, 121, 10504-10512.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10504-10512
    • Franz, K.J.1    Lippard, S.J.2
  • 21
    • 85085398682 scopus 로고    scopus 로고
    • Addition/Correction
    • Addition/Correction. J. Am. Chem. Soc. 2001, 123, 1266-1266.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1266-1266
  • 24
    • 0037473514 scopus 로고    scopus 로고
    • Molecular structure and conformation of dinitrosylheme
    • Conradie, J.; Wondimagegn, T.; Ghosh, A. Molecular structure and conformation of dinitrosylheme. J. Am. Chem. Soc. 2003, 125, 4968-4969.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4968-4969
    • Conradie, J.1    Wondimagegn, T.2    Ghosh, A.3
  • 25
    • 0034329425 scopus 로고    scopus 로고
    • Unprecedented proximal binding of nitric oxide to heme: Implications for guanylate cyclase
    • Lawson, D. M.; Stevenson, C. E. M.; Andrew, C. R.; Eady, R. R. Unprecedented proximal binding of nitric oxide to heme: Implications for guanylate cyclase. EMBO J. 2000, 19, 5661-5671.
    • (2000) EMBO J. , vol.19 , pp. 5661-5671
    • Lawson, D.M.1    Stevenson, C.E.M.2    Andrew, C.R.3    Eady, R.R.4
  • 26
    • 19744362699 scopus 로고    scopus 로고
    • Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break?
    • Marti, M. A.; Capece, L.; Crespo, A.; Doctorovich, F.; Estrin, D. A. Nitric oxide interaction with cytochrome c′ and its relevance to guanylate cyclase. Why does the iron histidine bond break? J. Am. Chem. Soc. 2005, 127, 7721-7728.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 7721-7728
    • Marti, M.A.1    Capece, L.2    Crespo, A.3    Doctorovich, F.4    Estrin, D.A.5
  • 27
    • 0002661813 scopus 로고
    • The organometqallic chemistry of transition-metal porphyrin complexes
    • Brothers, P.; Collman, J. P. The organometqallic chemistry of transition-metal porphyrin complexes. Acc. Chem. Res. 1986, 19, 209-215.
    • (1986) Acc. Chem. Res. , vol.19 , pp. 209-215
    • Brothers, P.1    Collman, J.P.2
  • 28
    • 0000755277 scopus 로고    scopus 로고
    • Organometallic chemistry of transition metal porphyrin complexes
    • Brothers, P. J. Organometallic chemistry of transition metal porphyrin complexes. Adv. Organomet. Chem. 2001, 46, 223-321.
    • (2001) Adv. Organomet. Chem. , vol.46 , pp. 223-321
    • Brothers, P.J.1
  • 29
    • 4043167669 scopus 로고    scopus 로고
    • Unique orbital symmetry-driven cisoid tilting of the axial ligands in dialkylruthenium(IV) porphyrins
    • Hansen, T.; Ovesen, H.; Svadberg, A.; Svendsen, K.; Tangen, E.; Swarts, J. C.; Ghosh, A. Unique orbital symmetry-driven cisoid tilting of the axial ligands in dialkylruthenium(IV) porphyrins. Organometallics 2004, 23, 3870-3872.
    • (2004) Organometallics , vol.23 , pp. 3870-3872
    • Hansen, T.1    Ovesen, H.2    Svadberg, A.3    Svendsen, K.4    Tangen, E.5    Swarts, J.C.6    Ghosh, A.7
  • 31
    • 84985520810 scopus 로고
    • Building bridges between inorganic and organic chemistry (Nobel lecture)
    • Hoffmann, R. Building bridges between inorganic and organic chemistry (Nobel lecture). Angew. Chem., Int. Ed. Engl. 1982, 21, 711-724.
    • (1982) Angew. Chem., Int. Ed. Engl. , vol.21 , pp. 711-724
    • Hoffmann, R.1
  • 33
    • 0035949448 scopus 로고    scopus 로고
    • Ligand-induced heme ruffling and bent NO geometry in ultra-high- resolution structures of nitrophorin 4
    • Roberts, S. A.; Weichsel, A.; Qiu, Y.; Shelnutt, J. A.; Walker, F. A.; Montfort, W. R. Ligand-induced heme ruffling and bent NO geometry in ultra-high-resolution structures of nitrophorin 4. Biochemistry 2001, 40, 11327-11337.
    • (2001) Biochemistry , vol.40 , pp. 11327-11337
    • Roberts, S.A.1    Weichsel, A.2    Qiu, Y.3    Shelnutt, J.A.4    Walker, F.A.5    Montfort, W.R.6
  • 35
    • 0034805264 scopus 로고    scopus 로고
    • A quantum chemical survey of metalloporphyrin-nitrosyl linkage isomers: Insights into the observation of multiple FeNO conformations in a recent crystallographic determination of nitrophorin 4
    • Wondimagegn, T.; Ghosh, A. A quantum chemical survey of metalloporphyrin-nitrosyl linkage isomers: Insights into the observation of multiple FeNO conformations in a recent crystallographic determination of nitrophorin 4. J. Am. Chem. Soc. 2001, 123, 5680-5683.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5680-5683
    • Wondimagegn, T.1    Ghosh, A.2
  • 36
    • 2442604589 scopus 로고    scopus 로고
    • Side-on copper-nitrosyl coordination by nitrite reductase
    • Tocheva, E. I.; Rosell, F. I.; Mauk, A. G.; Murphy, M. E. P. Side-on copper-nitrosyl coordination by nitrite reductase. Science 2004, 304, 867.
    • (2004) Science , vol.304 , pp. 867
    • Tocheva, E.I.1    Rosell, F.I.2    Mauk, A.G.3    Murphy, M.E.P.4
  • 37
    • 24744467360 scopus 로고    scopus 로고
    • Atomic resolution structures of resting-state, substrate-, and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism
    • Antonyuk, S. V.; Strange, R. W.; Sawers G.; Eady, R. R.; Hasnain, S. S. Atomic resolution structures of resting-state, substrate-, and product-complexed Cu-nitrite reductase provide insight into catalytic mechanism. Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 12041.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 12041
    • Antonyuk, S.V.1    Strange, R.W.2    Sawers, G.3    Eady, R.R.4    Hasnain, S.S.5
  • 38
    • 27644513403 scopus 로고    scopus 로고
    • Modeling side-on NO coordination to type 2 copper in nitrite reductase: Structures, energetics, and bonding
    • Wasbotten, A.; Ghosh, A. Modeling side-on NO coordination to type 2 copper in nitrite reductase: Structures, energetics, and bonding. J. Am. Chem. Soc. 2005, in press.
    • (2005) J. Am. Chem. Soc.
    • Wasbotten, A.1    Ghosh, A.2
  • 39
    • 0035587345 scopus 로고    scopus 로고
    • Mononitrosyl and trans-dinitrosyl complexes of phthalocyaninates of manganese and rhenium
    • Goldner, M.; Geniffke, B.; Franken, A.; Murray, K. S.; Homborg, H. Mononitrosyl and trans-dinitrosyl complexes of phthalocyaninates of manganese and rhenium. Z. Anorg. Allg. Chem. 2001, 627, 935-947.
    • (2001) Z. Anorg. Allg. Chem. , vol.627 , pp. 935-947
    • Goldner, M.1    Geniffke, B.2    Franken, A.3    Murray, K.S.4    Homborg, H.5
  • 40
    • 10444267330 scopus 로고    scopus 로고
    • 8 unit in a phthalocyanine complex: Some thoughts on dinitrosylheme intermediates in biology
    • 8 unit in a phthalocyanine complex: Some thoughts on dinitrosylheme intermediates in biology. J. Inorg. Biochem. 2005, 99, 55-59.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 55-59
    • Tangen, E.1    Conradie, J.2    Svadberg, A.3    Ghosh, A.4
  • 41
    • 37049099138 scopus 로고
    • Low-valent molybdenum porphyrin derivatives - Synthesis and X-ray crystal-structures of dinitrosyl and methanol(nitrosyl)-meso-tetra-para- tolylporphyrinatomolydenum(II) benzene solvates
    • Diebold, T.; Schappacher, M.; Chevrier, B.; Weiss, R. Low-valent molybdenum porphyrin derivatives - Synthesis and X-ray crystal-structures of dinitrosyl and methanol(nitrosyl)-meso-tetra-para-tolylporphyrinatomolydenum(II) benzene solvates. J. Chem. Soc. Chem. Commun. 1979, 16, 693-694.
    • (1979) J. Chem. Soc. Chem. Commun. , vol.16 , pp. 693-694
    • Diebold, T.1    Schappacher, M.2    Chevrier, B.3    Weiss, R.4
  • 42
    • 16244385332 scopus 로고    scopus 로고
    • 2, where P is a porphyrin: An organometallic perspective of metalloporphyrin-NO complexes
    • 2, where P is a porphyrin: An organometallic perspective of metalloporphyrin-NO complexes. J. Inorg. Biochem. 2005, 99, 959-962.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 959-962
    • Tangen, E.1    Ghosh, A.2
  • 43
    • 0037168603 scopus 로고    scopus 로고
    • Spin-dependent mechanism for diatomic ligand binding to heme
    • The discussion here is centered around binding equilibria. For a fascinating theoretical treatment of the kinetic aspects of diatomic ligand binding, see Franzen, S. Spin-dependent mechanism for diatomic ligand binding to heme. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 16754-16759.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 16754-16759
    • Franzen, S.1
  • 44
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • Gilles-Gonzalez, M. A.; Gonzalez, G. Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses. J. Inorg. Biochem. 2005, 99, 1-22.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 1-22
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 47
    • 3543102591 scopus 로고    scopus 로고
    • Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis
    • Karow, D. S.; Pan, D.; Tran, R.; Pellicena, P.; Presley, A.; Mathies, R. A.; Marletta, M. A. Spectroscopic characterization of the soluble guanylate cyclase-like heme domains from Vibrio cholerae and Thermoanaerobacter tengcongensis. Biochemistry 2004, 43, 10203-10211.
    • (2004) Biochemistry , vol.43 , pp. 10203-10211
    • Karow, D.S.1    Pan, D.2    Tran, R.3    Pellicena, P.4    Presley, A.5    Mathies, R.A.6    Marletta, M.A.7
  • 48
    • 4444333687 scopus 로고    scopus 로고
    • Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases
    • Pellicena, P.; Karow, D. S.; Boon, E. M.; Marletta, M. A.; Kuriyan, J. Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 12854-12859.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12854-12859
    • Pellicena, P.1    Karow, D.S.2    Boon, E.M.3    Marletta, M.A.4    Kuriyan, J.5
  • 49
    • 9444240366 scopus 로고    scopus 로고
    • Femtomolar sensitivity of a NO sensor from Clostridium botulinum
    • Nioche, P.; Berka, V.; Vipond, J.; Minton, N.; Tsai, A.-L.; Raman, C. S. Femtomolar sensitivity of a NO sensor from Clostridium botulinum. Science 2004, 306, 1550-1553.
    • (2004) Science , vol.306 , pp. 1550-1553
    • Nioche, P.1    Berka, V.2    Vipond, J.3    Minton, N.4    Tsai, A.-L.5    Raman, C.S.6
  • 50
    • 0141480853 scopus 로고    scopus 로고
    • Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane
    • Copeland, D. M.; West, A. H.; Richter-Addo, G. B. Crystal structures of ferrous horse heart myoglobin complexed with nitric oxide and nitrosoethane. Proteins: Struct., Funct., Genet. 2003, 53, 182-192.
    • (2003) Proteins: Struct., Funct., Genet. , vol.53 , pp. 182-192
    • Copeland, D.M.1    West, A.H.2    Richter-Addo, G.B.3
  • 51
  • 52
    • 0035476963 scopus 로고    scopus 로고
    • Non-VSEPR structures and bonding in d(0) systems
    • Our findings on unusual middle transition metal stereochemistries may be viewed as extending earlier findings on non-VSEPR early transition metal structures: Kaupp, M. Non-VSEPR structures and bonding in d(0) systems. Angew. Chem. Int. Ed. 2001, 40, 3535-3565.
    • (2001) Angew. Chem. Int. Ed. , vol.40 , pp. 3535-3565
    • Kaupp, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.