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Volumn 126, Issue 3, 1999, Pages 510-519

Azide- and cyanide-binding to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption, EPR and FTIR spectroscopies

Author keywords

Azide; bd type ubiquinol oxidase; Cyanide; EPR; FTIR

Indexed keywords

AZIDE; CYANIDE; CYTOCHROME B; HEME; OXIDOREDUCTASE;

EID: 0032823233     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022480     Document Type: Article
Times cited : (7)

References (53)
  • 1
    • 0040643267 scopus 로고    scopus 로고
    • Cytochrome bd terminal oxidase
    • Jünemann, S. (1997) Cytochrome bd terminal oxidase. Biochim. Biophys. Acta 1321, 107-127
    • (1997) Biochim. Biophys. Acta , vol.1321 , pp. 107-127
    • Jünemann, S.1
  • 2
    • 0031744093 scopus 로고    scopus 로고
    • Two terminal quinol oxidase families in Escherichia coli: Variations on molecular machinery for dioxygen reduction
    • Mogi, T., Tsubaki, M., Hori, H., Miyoshi, H., Nakamura, H., and Anraku, Y. (1998) Two terminal quinol oxidase families in Escherichia coli: Variations on molecular machinery for dioxygen reduction. J. Biochem. Mol. Biol. Biophys. 2, 79-110
    • (1998) J. Biochem. Mol. Biol. Biophys. , vol.2 , pp. 79-110
    • Mogi, T.1    Tsubaki, M.2    Hori, H.3    Miyoshi, H.4    Nakamura, H.5    Anraku, Y.6
  • 3
    • 0021099774 scopus 로고
    • The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain
    • Miller, M.J. and Gennis, R.B. (1983) The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J. Biol. Chem. 258, 9159-9165
    • (1983) J. Biol. Chem. , vol.258 , pp. 9159-9165
    • Miller, M.J.1    Gennis, R.B.2
  • 4
    • 0021272743 scopus 로고
    • 558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems
    • 558-d complex from cells grown with limited oxygen and evidence of branched electron-carrying systems. J. Biol. Chem. 259, 3375-3381
    • (1984) J. Biol. Chem. , vol.259 , pp. 3375-3381
    • Kita, K.1    Konishi, K.2    Anraku, Y.3
  • 6
    • 0023896679 scopus 로고
    • Synthesis of the heme d prosthetic group of bacterial terminal oxidase
    • Sotiriou, C. and Chang, C.K. (1988) Synthesis of the heme d prosthetic group of bacterial terminal oxidase. J. Am. Chem. Soc. 110, 2264-2270
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 2264-2270
    • Sotiriou, C.1    Chang, C.K.2
  • 7
    • 33845378891 scopus 로고
    • Proposed structure of heme d, a prosthetic group of bacterial terminal oxidases
    • Timkovich, R., Cork, M.S., Gennis, R.B., and Johnson, P.Y. (1985) Proposed structure of heme d, a prosthetic group of bacterial terminal oxidases. J. Am. Chem. Soc. 107, 6069-6075
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 6069-6075
    • Timkovich, R.1    Cork, M.S.2    Gennis, R.B.3    Johnson, P.Y.4
  • 8
    • 0024603308 scopus 로고
    • Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli
    • Lorence, R.M. and Gennis, R.B. (1989) Spectroscopic and quantitative analysis of the oxygenated and peroxy states of the purified cytochrome d complex of Escherichia coli. J. Biol. Chem. 264, 7135-7140
    • (1989) J. Biol. Chem. , vol.264 , pp. 7135-7140
    • Lorence, R.M.1    Gennis, R.B.2
  • 10
    • 0026337648 scopus 로고
    • Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectroscopy
    • Kahlow, M.A., Zuberi, T.M., Gennis, R.B., and Loehr, T.M. (1991) Identification of a ferryl intermediate of Escherichia coli cytochrome d terminal oxidase by resonance Raman spectroscopy. Biochemistry 30, 11485-11489
    • (1991) Biochemistry , vol.30 , pp. 11485-11489
    • Kahlow, M.A.1    Zuberi, T.M.2    Gennis, R.B.3    Loehr, T.M.4
  • 13
    • 0023650036 scopus 로고
    • Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli
    • Hata-Tanaka, A., Matsuura, K., Itoh, S., and Anraku, Y. (1987) Electron flow and heme-heme interaction between cytochromes b-558, b-595 and d in a terminal oxidase of Escherichia coli. Biochim. Biophys. Acta 893, 289-295
    • (1987) Biochim. Biophys. Acta , vol.893 , pp. 289-295
    • Hata-Tanaka, A.1    Matsuura, K.2    Itoh, S.3    Anraku, Y.4
  • 14
    • 0027299607 scopus 로고
    • Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli
    • Hill, J.J., Alben, J.O., and Gennis, R.B. (1993) Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli. Proc. Natl. Acad. Sci. USA 90, 5863-5867
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5863-5867
    • Hill, J.J.1    Alben, J.O.2    Gennis, R.B.3
  • 16
    • 0028791167 scopus 로고
    • Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli
    • Tsubaki, M., Hori, H., Mogi, T., and Anraku, Y. (1995) Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli. J. Biol. Chem. 270, 28565-28569
    • (1995) J. Biol. Chem. , vol.270 , pp. 28565-28569
    • Tsubaki, M.1    Hori, H.2    Mogi, T.3    Anraku, Y.4
  • 17
    • 0032867283 scopus 로고    scopus 로고
    • Fluoride-binding to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption and EPR spectroscopies
    • Tsubaki, M., Mogi, T., and Hori, H. (1999) Fluoride-binding to the Escherichia coli bd-type ubiquinol oxidase studied by visible absorption and EPR spectroscopies. J. Biochem. 126, 98-103
    • (1999) J. Biochem. , vol.126 , pp. 98-103
    • Tsubaki, M.1    Mogi, T.2    Hori, H.3
  • 18
    • 0024976978 scopus 로고
    • EPR studies of the cytochrome-d complex of Escherichia coli
    • Meinhardt, S.W., Gennis, R.B., and Ohnishi, T. (1989) EPR studies of the cytochrome-d complex of Escherichia coli. Biochim. Biophys. Acta 975, 175-184
    • (1989) Biochim. Biophys. Acta , vol.975 , pp. 175-184
    • Meinhardt, S.W.1    Gennis, R.B.2    Ohnishi, T.3
  • 19
    • 0024348253 scopus 로고
    • The cytochromes of anaerobically grown Escherichia coli. An electron-paramagnetic-resonance study of the cytochrome bd complex in situ
    • Rothery, R.A. and Ingledew, W.J. (1989) The cytochromes of anaerobically grown Escherichia coli. An electron-paramagnetic-resonance study of the cytochrome bd complex in situ. Biochem. J. 261, 437-443
    • (1989) Biochem. J. , vol.261 , pp. 437-443
    • Rothery, R.A.1    Ingledew, W.J.2
  • 20
    • 0014422622 scopus 로고
    • Analysis of a thermal equilibrium phenomenon between high-spin and low-spin states of ferrimyoglobin azide
    • Iizuka, T. and Kotani, M. (1968) Analysis of a thermal equilibrium phenomenon between high-spin and low-spin states of ferrimyoglobin azide. Biochim. Biophys. Acta 154, 417-419
    • (1968) Biochim. Biophys. Acta , vol.154 , pp. 417-419
    • Iizuka, T.1    Kotani, M.2
  • 21
    • 0027395144 scopus 로고
    • B binuclear site of bovine heart cytochrome c oxidase: Implication of the redox-linked conformational change at the binuclear site
    • B binuclear site of bovine heart cytochrome c oxidase: Implication of the redox-linked conformational change at the binuclear site. Biochemistry 32, 164-173
    • (1993) Biochemistry , vol.32 , pp. 164-173
    • Tsubaki, M.1
  • 22
    • 0027526880 scopus 로고
    • B binuclear site of bovine heart cytochrome c oxidase: New evidence for the redox-linked conformational change at the binuclear site
    • B binuclear site of bovine heart cytochrome c oxidase: New evidence for the redox-linked conformational change at the binuclear site. Biochemistry 32, 174-182
    • (1993) Biochemistry , vol.32 , pp. 174-182
    • Tsubaki, M.1
  • 23
    • 0015528143 scopus 로고
    • Infrared studies of azide bound to myoglobin and hemoglobin. Temperature dependence of ionicity
    • Alben, J.O. and Fager, L.Y. (1972) Infrared studies of azide bound to myoglobin and hemoglobin. Temperature dependence of ionicity. Biochemistry 11, 842-847
    • (1972) Biochemistry , vol.11 , pp. 842-847
    • Alben, J.O.1    Fager, L.Y.2
  • 25
    • 0026732663 scopus 로고
    • Electronic and stereochemical characterization of intermediates in the photolysis of ferric cytochrome P450scc nitrosyl complexes. Effects of cholesterol and its analogues on ligand binding structures
    • Hori, H., Masuya, F., Tsubaki, M., Yoshikawa, S., and Ichikawa, Y. (1992) Electronic and stereochemical characterization of intermediates in the photolysis of ferric cytochrome P450scc nitrosyl complexes. Effects of cholesterol and its analogues on ligand binding structures. J. Biol. Chem. 267, 18377-18381
    • (1992) J. Biol. Chem. , vol.267 , pp. 18377-18381
    • Hori, H.1    Masuya, F.2    Tsubaki, M.3    Yoshikawa, S.4    Ichikawa, Y.5
  • 26
    • 0027482992 scopus 로고
    • Cytochrome d axial ligand of the bd-type terminal quinol oxidase from Escherichia coli
    • Tsubaki, M., Uno, T., Hori, H., Mogi, T., Nishimura, Y., and Anraku, Y. (1993) Cytochrome d axial ligand of the bd-type terminal quinol oxidase from Escherichia coli. FEBS Lett. 335, 13-17
    • (1993) FEBS Lett. , vol.335 , pp. 13-17
    • Tsubaki, M.1    Uno, T.2    Hori, H.3    Mogi, T.4    Nishimura, Y.5    Anraku, Y.6
  • 27
    • 0027324414 scopus 로고
    • Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: EPR and Fourier-transform infrared spectroscopic studies
    • Tsubaki, M., Mogi, T., Anraku, Y., and Hori, H. (1993) Structure of the heme-copper binuclear center of the cytochrome bo complex of Escherichia coli: EPR and Fourier-transform infrared spectroscopic studies. Biochemistry 32, 6065-6072
    • (1993) Biochemistry , vol.32 , pp. 6065-6072
    • Tsubaki, M.1    Mogi, T.2    Anraku, Y.3    Hori, H.4
  • 28
    • 0029759829 scopus 로고    scopus 로고
    • 1 ground state which models the spectroscopic properties of heme d
    • 1 ground state which models the spectroscopic properties of heme d. J. Am. Chem. Soc. 118, 7373-7380
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7373-7380
    • Cheesman, M.R.1    Walker, F.A.2
  • 29
    • 0029942493 scopus 로고    scopus 로고
    • EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli: The proximal axial ligand of heme d is nitrogenous amino acid residue
    • Hori, H., Tsubaki, M., Mogi, T., and Anraku, Y. (1996) EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli: The proximal axial ligand of heme d is nitrogenous amino acid residue. J. Biol. Chem. 271, 9254-9258
    • (1996) J. Biol. Chem. , vol.271 , pp. 9254-9258
    • Hori, H.1    Tsubaki, M.2    Mogi, T.3    Anraku, Y.4
  • 30
    • 0000222176 scopus 로고
    • Iron(II, III)-chlorin and -isobacteriochlorin complexes. Models of the heme prosthetic groups in nitrite and sulfite reductases: Means of formation and spectroscopic and redox properties
    • Stolzenberg, A.M., Strauss, S.H., and Holm, R.H. (1981) Iron(II, III)-chlorin and -isobacteriochlorin complexes. Models of the heme prosthetic groups in nitrite and sulfite reductases: Means of formation and spectroscopic and redox properties. J. Am. Chem. Soc. 103, 4763-4778
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 4763-4778
    • Stolzenberg, A.M.1    Strauss, S.H.2    Holm, R.H.3
  • 31
    • 0015239532 scopus 로고
    • Sulf-heme proteins I. Optical and magnetic properties of sulfmyoglobin and its derivatives
    • Berzofsky, J.A., Peisach, J., and Blumberg, W.E. (1971) Sulf-heme proteins I. Optical and magnetic properties of sulfmyoglobin and its derivatives. J. Biol. Chem. 246, 3367-3377
    • (1971) J. Biol. Chem. , vol.246 , pp. 3367-3377
    • Berzofsky, J.A.1    Peisach, J.2    Blumberg, W.E.3
  • 32
    • 0000958014 scopus 로고
    • Iron chlorin-reconstituted histidine-ligated heme proteins as models for naturally occurring iron chlorin proteins: Magnetic circular dichroism spectroscopy as a probe of iron chlorin coordination structure
    • Bracete, A.M., Kadkhodayan, S., Sono, M., Huff, A.M., Zhuang, C., Cooper, D.K., Smith, K.M., Chang, C.K., and Dawson, J.H. (1994) Iron chlorin-reconstituted histidine-ligated heme proteins as models for naturally occurring iron chlorin proteins: Magnetic circular dichroism spectroscopy as a probe of iron chlorin coordination structure. Inorg. Chem. 33, 5042-5049
    • (1994) Inorg. Chem. , vol.33 , pp. 5042-5049
    • Bracete, A.M.1    Kadkhodayan, S.2    Sono, M.3    Huff, A.M.4    Zhuang, C.5    Cooper, D.K.6    Smith, K.M.7    Chang, C.K.8    Dawson, J.H.9
  • 33
    • 0000370757 scopus 로고
    • Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli
    • Koland, J.G., Miller, M.J., and Gennis, R.B. (1984) Potentiometric analysis of the purified cytochrome d terminal oxidase complex from Escherichia coli. J. Biol. Chem. 23, 1051-1056
    • (1984) J. Biol. Chem. , vol.23 , pp. 1051-1056
    • Koland, J.G.1    Miller, M.J.2    Gennis, R.B.3
  • 35
    • 0028134884 scopus 로고
    • The use of near-infrared charge-transfer transitions of low-spin ferric chlorins in axial ligand assignment
    • Peng, Q. and Peterson, J. (1994) The use of near-infrared charge-transfer transitions of low-spin ferric chlorins in axial ligand assignment. FEBS Lett. 356, 159-161
    • (1994) FEBS Lett. , vol.356 , pp. 159-161
    • Peng, Q.1    Peterson, J.2
  • 36
    • 0023643436 scopus 로고
    • Proton NMR characterization of isomeric sulfmyoglobins: Preparation, interconversion, reactivity patterns, and structural features
    • Chatfield, M.J., La Mar, G.N., and Kauten, R.J. (1987) Proton NMR characterization of isomeric sulfmyoglobins: Preparation, interconversion, reactivity patterns, and structural features. Biochemistry 26, 6939-6950
    • (1987) Biochemistry , vol.26 , pp. 6939-6950
    • Chatfield, M.J.1    La Mar, G.N.2    Kauten, R.J.3
  • 37
    • 0018308739 scopus 로고
    • Catalase of Neurospora crassa. 1. Induction, purification, and physical properties
    • Jacob, G.S. and Orme-Johnson, W.H. (1979) Catalase of Neurospora crassa. 1. Induction, purification, and physical properties. Biochemistry 18, 2967-2975
    • (1979) Biochemistry , vol.18 , pp. 2967-2975
    • Jacob, G.S.1    Orme-Johnson, W.H.2
  • 38
    • 0022623666 scopus 로고
    • An investigation of the ligand-binding properties of Pseudomonas aeruginosa nitrite reductase
    • Sutherland, J., Greenwood, C., Peterson, J., and Thomson, A.J. (1986) An investigation of the ligand-binding properties of Pseudomonas aeruginosa nitrite reductase. Biochem. J. 233, 893-898
    • (1986) Biochem. J. , vol.233 , pp. 893-898
    • Sutherland, J.1    Greenwood, C.2    Peterson, J.3    Thomson, A.J.4
  • 39
    • 0030571599 scopus 로고    scopus 로고
    • Reaction of E. coli catalase HPII with cyanide as ligand and as inhibitor
    • Maj, M., Nicholls, P., Obinger, C., Hillar, A., and Loewen, P.C. (1996) Reaction of E. coli catalase HPII with cyanide as ligand and as inhibitor. Biochim. Biophys. Acta 1298, 241-249
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 241-249
    • Maj, M.1    Nicholls, P.2    Obinger, C.3    Hillar, A.4    Loewen, P.C.5
  • 40
    • 0014938168 scopus 로고
    • Infrared studies of azido, cyano, and other derivatives of metmyoglobin, methemoglobin, and hemins
    • McCoy, S. and Caughey, W.S. (1970) Infrared studies of azido, cyano, and other derivatives of metmyoglobin, methemoglobin, and hemins. Biochemistry 9, 2387-2393
    • (1970) Biochemistry , vol.9 , pp. 2387-2393
    • McCoy, S.1    Caughey, W.S.2
  • 42
    • 0027439756 scopus 로고
    • Distinct forms of the haem o-Cu binuclear site of oxidised cytochrome bo from Escherichia coli. Evidence from optical and EPR spectroscopy
    • Watmough, N.J., Cheesman, M.R., Gennis, R.B., Greenwood, C., and Thomson, A.J. (1993) Distinct forms of the haem o-Cu binuclear site of oxidised cytochrome bo from Escherichia coli. Evidence from optical and EPR spectroscopy. FEBS Lett. 319, 151-154
    • (1993) FEBS Lett. , vol.319 , pp. 151-154
    • Watmough, N.J.1    Cheesman, M.R.2    Gennis, R.B.3    Greenwood, C.4    Thomson, A.J.5
  • 44
    • 0344481246 scopus 로고
    • Resonance Raman studies of the coupled binuclear copper active site in met azide hemocyanin
    • Pate, J.E., Thamann, T.J., and Solomon, E.I. (1986) Resonance Raman studies of the coupled binuclear copper active site in met azide hemocyanin. Spectrochim. Acta 42A, 313-318
    • (1986) Spectrochim. Acta , vol.42 A , pp. 313-318
    • Pate, J.E.1    Thamann, T.J.2    Solomon, E.I.3
  • 45
    • 0041117418 scopus 로고
    • Spectroscopic studies of the charge transfer and vibrational features of binuclear copper-(II) azide complexes: Comparison to the coupled binuclear copper active site in met azide hemocyanin and tyrosinase
    • Pate, J.E., Ross, P.K., Thamann, T.J., Reed, C.A., Karlin, K.D., Sorrell, T.N., and Solomon, E.I. (1989) Spectroscopic studies of the charge transfer and vibrational features of binuclear copper-(II) azide complexes: Comparison to the coupled binuclear copper active site in met azide hemocyanin and tyrosinase. J. Am. Chem. Soc. 111, 5198-5209
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5198-5209
    • Pate, J.E.1    Ross, P.K.2    Thamann, T.J.3    Reed, C.A.4    Karlin, K.D.5    Sorrell, T.N.6    Solomon, E.I.7
  • 46
    • 0032963684 scopus 로고    scopus 로고
    • Fourier-transform infrared studies on azide binding to the binuclear center of the Escherichia coli bo-type ubiquinol oxidase
    • Tsubaki, M., Mogi, T., and Hori, H. (1999) Fourier-transform infrared studies on azide binding to the binuclear center of the Escherichia coli bo-type ubiquinol oxidase. FEBS Lett. 449, 191-195
    • (1999) FEBS Lett. , vol.449 , pp. 191-195
    • Tsubaki, M.1    Mogi, T.2    Hori, H.3
  • 47
    • 0018318864 scopus 로고
    • Catalase of Neurospora crassa. 2. Electron paramagnetic resonance and chemical properties of the prosthetic group
    • Jacob, G.S. and Orme-Johnson, W.H. (1979) Catalase of Neurospora crassa. 2. Electron paramagnetic resonance and chemical properties of the prosthetic group. Biochemistry 18, 2975-2980
    • (1979) Biochemistry , vol.18 , pp. 2975-2980
    • Jacob, G.S.1    Orme-Johnson, W.H.2
  • 48
    • 0026348177 scopus 로고
    • The active site structure of E. coli HPII catalase. Evidence favoring coordination of a tyrosinate proximal ligand to the chlorin iron
    • Dawson, J.H., Bracete, A.M., Huff, A.M., Kadkhodayan, S., Zeitler, C.M., Sono, M., Chang, C.K., and Loewen, P.C. (1991) The active site structure of E. coli HPII catalase. Evidence favoring coordination of a tyrosinate proximal ligand to the chlorin iron. FEBS Lett. 295, 123-126
    • (1991) FEBS Lett. , vol.295 , pp. 123-126
    • Dawson, J.H.1    Bracete, A.M.2    Huff, A.M.3    Kadkhodayan, S.4    Zeitler, C.M.5    Sono, M.6    Chang, C.K.7    Loewen, P.C.8
  • 49
    • 0029062502 scopus 로고
    • Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site
    • Jünemann, S. and Wrigglesworth, J.M. (1995) Cytochrome bd oxidase from Azotobacter vinelandii. Purification and quantitation of ligand binding to the oxygen reduction site. J. Biol. Chem. 270, 16213-16220
    • (1995) J. Biol. Chem. , vol.270 , pp. 16213-16220
    • Jünemann, S.1    Wrigglesworth, J.M.2
  • 50
    • 0026793499 scopus 로고
    • Identification of heme macrocycle type by near-infrared magnetic circular dichroism spectroscopy at cryogenic temperatures
    • Peng, Q., Timkovich, R., Loewen, P.C., and Peterson, J. (1992) Identification of heme macrocycle type by near-infrared magnetic circular dichroism spectroscopy at cryogenic temperatures. FEBS Lett. 309, 157-160
    • (1992) FEBS Lett. , vol.309 , pp. 157-160
    • Peng, Q.1    Timkovich, R.2    Loewen, P.C.3    Peterson, J.4
  • 51
    • 0033547815 scopus 로고    scopus 로고
    • Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands
    • Borisov, V., Arutyunyan, A.M., Osborne, J.P., Gennis, R.B., and Konstantinov, A.A. (1999) Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands. Biochemistry 38, 740-750
    • (1999) Biochemistry , vol.38 , pp. 740-750
    • Borisov, V.1    Arutyunyan, A.M.2    Osborne, J.P.3    Gennis, R.B.4    Konstantinov, A.A.5
  • 52
    • 0029121227 scopus 로고
    • Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as-isolated" enzyme and characterization of the cyanide adduct
    • Sun, J., Oscorne, J.P., Kahlow, M.A., Kaysser, T.M., Gennis, R.B., and Loehr, T.M. (1995) Resonance Raman studies of Escherichia coli cytochrome bd oxidase. Selective enhancement of the three heme chromophores of the "as-isolated" enzyme and characterization of the cyanide adduct. Biochemistry 34, 12144-12151
    • (1995) Biochemistry , vol.34 , pp. 12144-12151
    • Sun, J.1    Oscorne, J.P.2    Kahlow, M.A.3    Kaysser, T.M.4    Gennis, R.B.5    Loehr, T.M.6


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