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Volumn 50, Issue 26, 2011, Pages 5939-5947

Spectroscopic characterization of mononitrosyl complexes in heme-nonheme diiron centers within the myoglobin scaffold (FeBMbs): Relevance to denitrifying No reductase

Author keywords

[No Author keywords available]

Indexed keywords

APOPROTEINS; BOUND PROTEINS; ENGINEERED SITE; FT-IR SPECTRUM; FTIR SPECTROSCOPY; GLUTAMIC ACID; HEME-COPPER TERMINALS; LIQUID NITROGEN TEMPERATURE; NO MOLECULE; NONHEME; RESONANCE RAMAN; RESONANCE RAMAN SPECTRA; SPECTROSCOPIC CHARACTERIZATION; SPERM WHALES; TRANS-MEMBRANE PROTEINS; UV-VIS ABSORPTIONS; VIBRATIONAL MODES;

EID: 79959808611     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200409a     Document Type: Article
Times cited : (34)

References (36)
  • 2
    • 10444275550 scopus 로고    scopus 로고
    • Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type
    • DOI 10.1016/j.jinorgbio.2004.09.024, PII S0162013404002909, Heme-Diatomic Interactions, Part 1
    • Zumft, W. G. (2005) Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme-copper oxidase type J. Inorg. Biochem. 99, 194-215 (Pubitemid 39642979)
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 194-215
    • Zumft, W.G.1
  • 3
    • 34249789578 scopus 로고    scopus 로고
    • Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins
    • DOI 10.1039/b604194a
    • Moënne-Loccoz, P. (2007) Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins Nat. Prod. Rep. 24, 610-620 (Pubitemid 46848713)
    • (2007) Natural Product Reports , vol.24 , Issue.3 , pp. 610-620
    • Moenne-Loccoz, P.1
  • 4
    • 33750479893 scopus 로고    scopus 로고
    • Involvement of nitric oxide in biofilm dispersal of Pseudomonas aeruginosa
    • DOI 10.1128/JB.00779-06
    • Barraud, N., Hassett, D. J., Hwang, S. H., Rice, S. A., Kjelleberg, S., and Webb, J. S. (2006) Involvement of nitric oxide in biofilm dispersal of Pseudomonas aeruginosa J. Bacteriol. 188, 7344-7353 (Pubitemid 44646233)
    • (2006) Journal of Bacteriology , vol.188 , Issue.21 , pp. 7344-7353
    • Barraud, N.1    Hassett, D.J.2    Hwang, S.-H.3    Rice, S.A.4    Kjelleberg, S.5    Webb, J.S.6
  • 5
    • 34250327396 scopus 로고    scopus 로고
    • Metabolism of nitric oxide by Neisseria meningitidis modifies release of NO-regulated cytokines and chemokines by human macrophages
    • DOI 10.1016/j.micinf.2007.04.002, PII S1286457907001633
    • Stevanin, T. M., Laver, J. R., Poole, R. K., Moir, J. W., and Read, R. C. (2007) Metabolism of nitric oxide by Neisseria meningitidis modifies release of NO-regulated cytokines and chemokines by human macrophages Microbes Infect. 9, 981-987 (Pubitemid 46921019)
    • (2007) Microbes and Infection , vol.9 , Issue.8 , pp. 981-987
    • Stevanin, T.M.1    Laver, J.R.2    Poole, R.K.3    Moir, J.W.B.4    Read, R.C.5
  • 8
    • 0029988772 scopus 로고    scopus 로고
    • Cytochrome cb-type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512
    • Fujiwara, T. and Fukumori, Y. (1996) Cytochrome cb -type nitric oxide reductase with cytochrome c oxidase activity from Paracoccus denitrificans ATCC 35512 J. Bacteriol. 178, 1866-1871 (Pubitemid 26110528)
    • (1996) Journal of Bacteriology , vol.178 , Issue.7 , pp. 1866-1871
    • Fujiwara, T.1    Fukumori, Y.2
  • 14
    • 33745203021 scopus 로고    scopus 로고
    • Reduction of nitric oxide in bacterial nitric oxide reductase: A theoretical model study
    • Blomberg, L. M., Blomberg, M. R., and Siegbahn, P. E. (2006) Reduction of nitric oxide in bacterial nitric oxide reductase: A theoretical model study Biochim. Biophys. Acta 1757, 240-252
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 240-252
    • Blomberg, L.M.1    Blomberg, M.R.2    Siegbahn, P.E.3
  • 16
    • 77952700938 scopus 로고    scopus 로고
    • Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin
    • Lin, Y. W., Yeung, N., Gao, Y. G., Miner, K. D., Tian, S., Robinson, H., and Lu, Y. (2010) Roles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobin Proc. Natl. Acad. Sci. U.S.A. 107, 8581-8586
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 8581-8586
    • Lin, Y.W.1    Yeung, N.2    Gao, Y.G.3    Miner, K.D.4    Tian, S.5    Robinson, H.6    Lu, Y.7
  • 17
    • 0018792074 scopus 로고
    • Assignment of the Fe-Ne (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin
    • Kitagawa, T., Nagai, K., and Tsubaki, M. (1979) Assignment of the Fe-Ne (His F8) stretching band in the resonance Raman spectra of deoxy myoglobin FEBS Lett. 104, 376-378
    • (1979) FEBS Lett. , vol.104 , pp. 376-378
    • Kitagawa, T.1    Nagai, K.2    Tsubaki, M.3
  • 19
    • 76149125163 scopus 로고    scopus 로고
    • Role of copper ion in regulating ligand binding in a myoglobin-based cytochrome c oxidase model
    • Lu, C., Zhao, X., Lu, Y., Rousseau, D. L., and Yeh, S. R. (2010) Role of copper ion in regulating ligand binding in a myoglobin-based cytochrome c oxidase model J. Am. Chem. Soc. 132, 1598-1605
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1598-1605
    • Lu, C.1    Zhao, X.2    Lu, Y.3    Rousseau, D.L.4    Yeh, S.R.5
  • 20
    • 0015514831 scopus 로고
    • Circular dichroism studies of myoglobin and cytochrome c derivatives
    • Bolard, J. and Garnier, A. (1972) Circular dichroism studies of myoglobin and cytochrome c derivatives Biochim. Biophys. Acta 263, 535-549
    • (1972) Biochim. Biophys. Acta , vol.263 , pp. 535-549
    • Bolard, J.1    Garnier, A.2
  • 21
    • 0017193799 scopus 로고
    • Equilibrium between six- and five-coordinated hemes in nitrosylhemoglobin: Interpretation of electron spin resonance spectra
    • Szabo, A. and Perutz, M. F. (1976) Equilibrium between six- and five-coordinated hemes in nitrosylhemoglobin: Interpretation of electron spin resonance spectra Biochemistry 15, 4427-4428
    • (1976) Biochemistry , vol.15 , pp. 4427-4428
    • Szabo, A.1    Perutz, M.F.2
  • 22
    • 0000729344 scopus 로고
    • Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: Detection of Fe(III)-NO stretching, Fe(III)-N-O bending, and Fe(II)-N-O bending vibrations
    • Benko, B. and Yu, N. T. (1983) Resonance Raman studies of nitric oxide binding to ferric and ferrous hemoproteins: Detection of Fe(III)-NO stretching, Fe(III)-N-O bending, and Fe(II)-N-O bending vibrations Proc. Natl. Acad. Sci. U.S.A. 80, 7042-7046 (Pubitemid 14225214)
    • (1983) Proceedings of the National Academy of Sciences of the United States of America , vol.80 , Issue.22 , pp. 7042-7046
    • Benko, B.1    Yu, N.T.2
  • 23
    • 0020484829 scopus 로고
    • Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: Detection of bound N-O stretching and Fe-NO stretching vibrations from the hexacoordinated NO-heme complex
    • Tsubaki, M. and Yu, N. T. (1982) Resonance Raman investigation of nitric oxide bonding in nitrosylhemoglobin A and -myoglobin: Detection of bound N-O stretching and Fe-NO stretching vibrations from the hexacoordinated NO-heme complex Biochemistry 21, 1140-1144
    • (1982) Biochemistry , vol.21 , pp. 1140-1144
    • Tsubaki, M.1    Yu, N.T.2
  • 24
    • 9644302978 scopus 로고    scopus 로고
    • Two CO molecules can bind concomitantly at the diiron site of NO reductase from Bacillus azotoformans
    • Lu, S., Suharti, de Vries, S., and Moënne-Loccoz, P. (2004) Two CO molecules can bind concomitantly at the diiron site of NO reductase from Bacillus azotoformans J. Am. Chem. Soc. 126, 15332-15333 (Pubitemid 39577439)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.47 , pp. 15332-15333
    • Lu, S.1    Suharti2    De Vries, S.3    Moenne-Loccoz, P.4
  • 25
    • 0030774809 scopus 로고    scopus 로고
    • Identification of conformational substates involved in nitric oxide binding to ferric and ferrous myoglobin through difference fourier transform infrared spectroscopy (FTIR)
    • DOI 10.1021/bi962744o
    • Miller, L. M., Pedraza, A. J., and Chance, M. R. (1997) Identification of conformational substates involved in nitric oxide binding to ferric and ferrous myoglobin through difference Fourier transform infrared spectroscopy (FTIR) Biochemistry 36, 12199-12207 (Pubitemid 27440957)
    • (1997) Biochemistry , vol.36 , Issue.40 , pp. 12199-12207
    • Miller, L.M.1    Pedraza, A.J.2    Chance, M.R.3
  • 27
    • 0003178953 scopus 로고
    • Resonance Raman spectra of nitrosyl heme proteins and of porphyrin analogues
    • Stong, J. D., Burke, J. M., Daly, P., Wright, P., and Spiro, T. G. (1980) Resonance Raman spectra of nitrosyl heme proteins and of porphyrin analogues J. Am. Chem. Soc. 102, 5815-5819
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 5815-5819
    • Stong, J.D.1    Burke, J.M.2    Daly, P.3    Wright, P.4    Spiro, T.G.5
  • 29
    • 77954995956 scopus 로고    scopus 로고
    • Oriented single-crystal nuclear resonance vibrational spectroscopy of [Fe(TPP)(MI)(NO)]: Quantitative assessment of the trans effect of NO
    • Lehnert, N., Sage, J. T., Silvernail, N., Scheidt, W. R., Alp, E. E., Sturhahn, W., and Zhao, J. (2010) Oriented single-crystal nuclear resonance vibrational spectroscopy of [Fe(TPP)(MI)(NO)]: Quantitative assessment of the trans effect of NO Inorg. Chem. 49, 7197-7215
    • (2010) Inorg. Chem. , vol.49 , pp. 7197-7215
    • Lehnert, N.1    Sage, J.T.2    Silvernail, N.3    Scheidt, W.R.4    Alp, E.E.5    Sturhahn, W.6    Zhao, J.7
  • 31
    • 0035846626 scopus 로고    scopus 로고
    • FTIR and resonance raman studies of nitric oxide binding to H93G cavity mutants of myoglobin
    • DOI 10.1021/bi011440l
    • Thomas, M. R., Brown, D., Franzen, S., and Boxer, S. G. (2001) FTIR and resonance Raman studies of nitric oxide binding to H93G cavity mutants of myoglobin Biochemistry 40, 15047-15056 (Pubitemid 33136128)
    • (2001) Biochemistry , vol.40 , Issue.49 , pp. 15047-15056
    • Thomas, M.R.1    Brown, D.2    Franzen, S.3    Boxer, S.G.4
  • 32
    • 33845952634 scopus 로고    scopus 로고
    • Differential sensing of protein influences by NO and CO vibrations in heme adducts
    • DOI 10.1021/ja064859d
    • Ibrahim, M., Xu, C., and Spiro, T. G. (2006) Differential sensing of protein influences by NO and CO vibrations in heme adducts J. Am. Chem. Soc. 128, 16834-16845 (Pubitemid 46032759)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.51 , pp. 16834-16845
    • Ibrahim, M.1    Xu, C.2    Spiro, T.G.3
  • 33
    • 0033520701 scopus 로고    scopus 로고
    • Determinants of the FeXO (X = C, N, O) vibrational frequencies in heme adducts from experiment and density function theory
    • Vogel, K. M., Kozlowski, P. M., Zgierski, M. Z., and Spiro, T. G. (1999) Determinants of the FeXO (X = C, N, O) vibrational frequencies in heme adducts from experiment and density function theory J. Am. Chem. Soc. 121, 9915-9921
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9915-9921
    • Vogel, K.M.1    Kozlowski, P.M.2    Zgierski, M.Z.3    Spiro, T.G.4
  • 34
    • 0037133132 scopus 로고    scopus 로고
    • Proton and electron pathways in the bacterial nitric oxide reductase
    • DOI 10.1021/bi0121050
    • Hendriks, J. H., Jasaitis, A., Saraste, M., and Verkhovsky, M. I. (2002) Proton and electron pathways in the bacterial nitric oxide reductase Biochemistry 41, 2331-2340 (Pubitemid 34160895)
    • (2002) Biochemistry , vol.41 , Issue.7 , pp. 2331-2340
    • Hendriks, J.H.M.1    Jasaitis, A.2    Saraste, M.3    Verkhovsky, M.I.4
  • 35
    • 11244302439 scopus 로고    scopus 로고
    • NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: Characterization of reaction intermediates that appear in the single turnover cycle
    • DOI 10.1074/jbc.M409996200
    • Kumita, H., Matsuura, K., Hino, T., Takahashi, S., Hori, H., Fukumori, Y., Morishima, I., and Shiro, Y. (2004) NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: Characterization of reaction intermediates that appear in the single turnover cycle J. Biol. Chem. 279, 55247-55254 (Pubitemid 40066521)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.53 , pp. 55247-55254
    • Kumita, H.1    Matsuura, K.2    Hino, T.3    Takahashi, S.4    Hori, H.5    Fukumori, Y.6    Morishima, I.7    Shiro, Y.8
  • 36
    • 0001652725 scopus 로고    scopus 로고
    • Resonance Raman investigation of Fe-N-O structure of nitrosylheme in myoglobin and its mutants
    • Tomita, T., Hirota, S., Ogura, T., Olson, J. S., and Kitagawa, T. (1999) Resonance Raman investigation of Fe-N-O structrue of nitrosylheme in myoglobin and its mutants J. Phys. Chem. B 103, 7044-7054 (Pubitemid 129702490)
    • (1999) Journal of Physical Chemistry B , vol.103 , Issue.33 , pp. 7044-7054
    • Tomita, T.1    Hirota, S.2    Ogura, T.3    Olson, J.S.4    Kitagawa, T.5


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