메뉴 건너뛰기




Volumn 293, Issue , 2014, Pages 81-87

Static quenching of tryptophan fluorescence in proteins by a dioxomolybdenum(VI) thiolate complex

Author keywords

Molybdenum complex; Serum albumins; Static quenching; Tryptophan fluorescence

Indexed keywords


EID: 84906243580     PISSN: 10106030     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotochem.2014.07.023     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 0022987651 scopus 로고
    • A spectroscopic study of nickel (II)-bovine serum albumin binding and reactivity
    • S.H. Laurie, and D.E. Pratt A spectroscopic study of nickel (II)-bovine serum albumin binding and reactivity J. Inorg. Biochem. 28 1986 431 439
    • (1986) J. Inorg. Biochem. , vol.28 , pp. 431-439
    • Laurie, S.H.1    Pratt, D.E.2
  • 3
    • 84857533934 scopus 로고    scopus 로고
    • Quenching of tryptophan fluorescence in various proteins by a series of small nickel complexes
    • H.F. Crouse, J. Potoma, F. Nejrabi, D.L. Snyder, B.S. Chohan, and S. Basu Quenching of tryptophan fluorescence in various proteins by a series of small nickel complexes Dalton Trans. 41 2012 2720 2731
    • (2012) Dalton Trans. , vol.41 , pp. 2720-2731
    • Crouse, H.F.1    Potoma, J.2    Nejrabi, F.3    Snyder, D.L.4    Chohan, B.S.5    Basu, S.6
  • 4
    • 79957858638 scopus 로고    scopus 로고
    • Static and dynamic quenching of tryptophan fluorescence in various proteins by a chromium (III) complex
    • H.F. Crouse, E.M. Petrunak, A.M. Donovan, A.C. Merkle, B.L. Swartz, and S. Basu Static and dynamic quenching of tryptophan fluorescence in various proteins by a chromium (III) complex Spectrosc. Lett. 44 2011 369 374
    • (2011) Spectrosc. Lett. , vol.44 , pp. 369-374
    • Crouse, H.F.1    Petrunak, E.M.2    Donovan, A.M.3    Merkle, A.C.4    Swartz, B.L.5    Basu, S.6
  • 5
    • 2442516167 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer from tryptophan to a chromium(III) complex accompanied by non-specific cleavage of albumin: A step forward towards the development of a novel photoprotease
    • DOI 10.1016/j.jinorgbio.2004.02.014, PII S0162013404000509
    • H.Y. Shrivastava, and B.U. Nair Fluorescence resonance energy transfer from tryptophan to a chromium (III) complex accompanied by non-specific cleavage of albumin: a step forward towards the development of a novel photoprotease J. Inorg. Biochem. 98 2004 991 994 (Pubitemid 38638495)
    • (2004) Journal of Inorganic Biochemistry , vol.98 , Issue.6 , pp. 991-994
    • Shrivastava, H.Y.1    Nair, B.U.2
  • 6
    • 27544457208 scopus 로고    scopus 로고
    • Quenching of the intrinsic fluorescence of bovine serum albumin by phenylfluorone-Mo(VI) complex as a probe
    • W. Dan, W. Qin, L. Yan, D. Bin, and X. Guiying Quenching of the intrinsic fluorescence of bovine serum albumin by phenylfluorone-Mo(VI) complex as a probe Int. J. Biol. Macromol. 37 2005 69 72
    • (2005) Int. J. Biol. Macromol. , vol.37 , pp. 69-72
    • Dan, W.1    Qin, W.2    Yan, L.3    Bin, D.4    Guiying, X.5
  • 7
    • 32144451207 scopus 로고    scopus 로고
    • Interaction of m-nitrophenylfluorone-Mo(VI) complex as a probe with human serum albumin: A fluorescence quenching study
    • W. Qin, W. Dan, D. Bin, L. Yan, and D. Caihong Interaction of m-nitrophenylfluorone-Mo(VI) complex as a probe with human serum albumin: a fluorescence quenching study Spectrochim. Acta A: Mol. Biomol. Spectrosc. 63 2006 532 535
    • (2006) Spectrochim. Acta A: Mol. Biomol. Spectrosc. , vol.63 , pp. 532-535
    • Qin, W.1    Dan, W.2    Bin, D.3    Yan, L.4    Caihong, D.5
  • 9
    • 0026041957 scopus 로고
    • The role of albumin in human physiology and pathophysiology, Part III: Albumin and disease states
    • J.P. Doweiko, and D.J. Nompleggi The role of albumin in human physiology and pathophysiology, Part III: Albumin and disease states J. Parenter. Enteral. Nutr. 15 1991 476 483
    • (1991) J. Parenter. Enteral. Nutr. , vol.15 , pp. 476-483
    • Doweiko, J.P.1    Nompleggi, D.J.2
  • 11
    • 0025829605 scopus 로고
    • Role of albumin in human physiology and pathophysiology
    • J.P. Doweiko, and D.J. Nompleggi Role of albumin in human physiology and pathophysiology J. Parenter. Enteral. Nutr. 15 1991 207 211
    • (1991) J. Parenter. Enteral. Nutr. , vol.15 , pp. 207-211
    • Doweiko, J.P.1    Nompleggi, D.J.2
  • 12
    • 0028558671 scopus 로고
    • Preliminary crystallographic studies of four crystal forms of serum albumin
    • D.C. Carter, B. Chang, J.X. Ho, K. Keeling, and Z. Krishnasami Preliminary crystallographic studies of four crystal forms of serum albumin Eur. J. Biochem. 226 1994 1049 1052
    • (1994) Eur. J. Biochem. , vol.226 , pp. 1049-1052
    • Carter, D.C.1    Chang, B.2    Ho, J.X.3    Keeling, K.4    Krishnasami, Z.5
  • 13
    • 0025301143 scopus 로고
    • Structure of human serum albumin
    • D.C. Carter, and X.M. He Structure of human serum albumin Science 249 1990 302 303 (Pubitemid 20232094)
    • (1990) Science , vol.249 , Issue.4966 , pp. 302-303
    • Carter, D.C.1    He, X.-M.2
  • 15
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • X.M. He, and D.C. Carter Atomic structure and chemistry of human serum albumin Nature 358 1992 209 215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 16
    • 5444272528 scopus 로고    scopus 로고
    • Properties of crosslinked protein matrices for tissue engineering applications synthesized by multiphoton excitation
    • DOI 10.1002/jbm.a.30174
    • S. Basu, and P.J. Campagnola Properties of crosslinked protein matrices for tissue engineering applications synthesized by multiphoton excitation J. Biomed. Mater. Res. A 71 2004 359 368 (Pubitemid 39362918)
    • (2004) Journal of Biomedical Materials Research - Part A , vol.71 , Issue.2 , pp. 359-368
    • Basu, S.1    Campagnola, P.J.2
  • 17
    • 1342343021 scopus 로고    scopus 로고
    • Study of the interaction of kaempferol with bovine serum albumin
    • T. Jianniao, L.-J. Qin, T. Xuan, H. Zhide, and C.-X. Guo Study of the interaction of kaempferol with bovine serum albumin J. Mol. Struct. 691 2004 197 202
    • (2004) J. Mol. Struct. , vol.691 , pp. 197-202
    • Jianniao, T.1    Qin, L.-J.2    Xuan, T.3    Zhide, H.4    Guo, C.-X.5
  • 18
    • 0016696047 scopus 로고
    • Tryptophan fluorescence lifetimes in lysozyme
    • C. Formoso, and L.S. Forster Tryptophan fluorescence lifetimes in lysozyme J. Biol. Chem. 250 1975 3738 3745
    • (1975) J. Biol. Chem. , vol.250 , pp. 3738-3745
    • Formoso, C.1    Forster, L.S.2
  • 19
    • 0015343130 scopus 로고
    • Fluorescence of lysozyme: Emissions from tryptophan residues 62 and 108 and energy migration
    • T. Imoto, L.S. Forster, J.A. Rupley, and F. Tanaka Fluorescence of lysozyme: emissions from tryptophan residues 62 and 108 and energy migration Proc. Natl. Acad. Sci. U. S. A. 69 1972 1151 1155
    • (1972) Proc. Natl. Acad. Sci. U. S. A. , vol.69 , pp. 1151-1155
    • Imoto, T.1    Forster, L.S.2    Rupley, J.A.3    Tanaka, F.4
  • 21
    • 33748413614 scopus 로고    scopus 로고
    • Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence
    • DOI 10.1002/mnfr.200600013
    • H.M. Rawel, S.K. Frey, K. Meidtner, J. Kroll, and F.J. Schweigert Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence Mol. Nutr. Food Res. 50 2006 705 713 (Pubitemid 44342467)
    • (2006) Molecular Nutrition and Food Research , vol.50 , Issue.8 , pp. 705-713
    • Rawel, H.M.1    Frey, S.K.2    Meidtner, K.3    Kroll, J.4    Schweigert, F.J.5
  • 22
    • 34249815534 scopus 로고    scopus 로고
    • Interactions of lysozyme with 6-amino-4-aryl-3-methyl-1-phenyl-1H- pyrazolo[3,4-b]pyridine-5-carbonitriles: A fluorescence quenching study
    • W. Hin, L.-S. Qin, S. Yang, and W. Yu Interactions of lysozyme with 6-amino-4-aryl-3-methyl-1-phenyl-1H-pyrazolo[3,4-b]pyridine-5-carbonitriles: a fluorescence quenching study Anal. Sci. 23 2007 419 422
    • (2007) Anal. Sci. , vol.23 , pp. 419-422
    • Hin, W.1    Qin, L.-S.2    Yang, S.3    Yu, W.4
  • 23
    • 23444447825 scopus 로고    scopus 로고
    • Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method
    • DOI 10.1016/j.molstruc.2005.04.032, PII S0022286005003753
    • Y.-J. Hu, Y. Liu, L.-X. Zhang, R.-M. Zhao, and S.-S. Qu Studies of interaction between colchicine and bovine serum albumin by fluorescence quenching method J. Mol. Struct. 750 2005 174 178 (Pubitemid 41112331)
    • (2005) Journal of Molecular Structure , vol.750 , Issue.1-3 , pp. 174-178
    • Hu, Y.-J.1    Liu, Y.2    Zhang, L.-X.3    Zhao, R.-M.4    Qu, S.-S.5
  • 25
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • M.R. Eftink, and C.A. Ghiron Fluorescence quenching studies with proteins Anal. Biochem. 114 1981 199 227
    • (1981) Anal. Biochem. , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 29
    • 33747619382 scopus 로고    scopus 로고
    • Quenching of the intrinsic fluorescence of human serum albumin by trimethoxyphenylfluorone-Mo(VI) complex
    • W. Dan, D. Bin, M.-H. Min, W. Qin, and X.-G. Ying Quenching of the intrinsic fluorescence of human serum albumin by trimethoxyphenylfluorone-Mo(VI) complex Spectrosc. Lett. 39 2006 399 408
    • (2006) Spectrosc. Lett. , vol.39 , pp. 399-408
    • Dan, W.1    Bin, D.2    Min, M.-H.3    Qin, W.4    Ying, X.-G.5
  • 30
    • 0040058823 scopus 로고
    • Oxygen atom transfer reactions. Epoxide deoxygenation by bis(diethyldithiocarbamato)oxomolybdenum
    • K.G. Moloy Oxygen atom transfer reactions. Epoxide deoxygenation by bis(diethyldithiocarbamato)oxomolybdenum Inorg. Chem. 27 1988 677 681
    • (1988) Inorg. Chem. , vol.27 , pp. 677-681
    • Moloy, K.G.1
  • 31
    • 0001421826 scopus 로고
    • Dialkyldithiocarbamate complexes of molybdenum(V) and molybdenum(VI)
    • F.W. Moore, and M.L. Larson Dialkyldithiocarbamate complexes of molybdenum(V) and molybdenum(VI) Inorg. Chem. 6 1967 998 1003
    • (1967) Inorg. Chem. , vol.6 , pp. 998-1003
    • Moore, F.W.1    Larson, M.L.2
  • 33
    • 84961986830 scopus 로고    scopus 로고
    • Revisiting fluorenone photophysics via dipolar fluorenone derivatives
    • L.A. Estrada, J.E. Yarnell, and D.C. Neckers Revisiting fluorenone photophysics via dipolar fluorenone derivatives J. Phys. Chem. A 115 2011 6366 6375
    • (2011) J. Phys. Chem. A , vol.115 , pp. 6366-6375
    • Estrada, L.A.1    Yarnell, J.E.2    Neckers, D.C.3
  • 36
    • 84857789666 scopus 로고    scopus 로고
    • Hydrogen bonding in the electronic excited state
    • G.-J. Zhao, and K.-L. Han Hydrogen bonding in the electronic excited state Acc. Chem. Res. 45 2012 404 413
    • (2012) Acc. Chem. Res. , vol.45 , pp. 404-413
    • Zhao, G.-J.1    Han, K.-L.2
  • 37
    • 34548206307 scopus 로고    scopus 로고
    • Site-selective photoinduced electron transfer from alcoholic solvents to the chromophore facilitated by hydrogen bonding: A new fluorescence quenching mechanism
    • DOI 10.1021/jp0734530
    • G.-J. Zhao, J.-Y. Liu, L.-C. Zhou, and K.-L. Han Site-selective photoinduced electron transfer from alcoholic solvents to the chromophore facilitated by hydrogen bonding: a new fluorescence quenching mechanism J. Phys. Chem. B 111 2007 8940 8945 (Pubitemid 47317473)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.30 , pp. 8940-8945
    • Zhao, G.-J.1    Liu, J.-Y.2    Zhou, L.-C.3    Han, K.-L.4
  • 38
    • 0000012892 scopus 로고
    • DSC studies on the denaturation and aggregation of serum albumins
    • G. Barone, C. Giancola, and A. Verdoliva DSC studies on the denaturation and aggregation of serum albumins Thermochim. Acta 199 1992 197 205
    • (1992) Thermochim. Acta , vol.199 , pp. 197-205
    • Barone, G.1    Giancola, C.2    Verdoliva, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.