메뉴 건너뛰기




Volumn 336, Issue 1, 2005, Pages 210-214

Roles of Trp144 and Tyr203 in copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013

Author keywords

Copper protein; Denitrification; Electron transfer; Metalloenzyme; Nitrite reductase; Redox

Indexed keywords

AZURIN; COPPER DERIVATIVE; NITRITE REDUCTASE; TRYPTOPHAN; TYROSINE;

EID: 24344505512     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.076     Document Type: Article
Times cited : (11)

References (26)
  • 1
    • 0031456471 scopus 로고    scopus 로고
    • Cell biology and molecular basis of denitrification
    • W.G. Zumft Cell biology and molecular basis of denitrification Microbiol. Mol. Biol. Rev. 61 1997 533 616
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 2
    • 17944403239 scopus 로고    scopus 로고
    • Structure-function relationships of copper-containing nitrite reductases
    • S. Suzuki, K. Kataoka, K. Yamaguchi, T. Inoue, and Y. Kai Structure-function relationships of copper-containing nitrite reductases Coord. Chem. Rev. 190-192 1999 245 265
    • (1999) Coord. Chem. Rev. , vol.190-192 , pp. 245-265
    • Suzuki, S.1    Kataoka, K.2    Yamaguchi, K.3    Inoue, T.4    Kai, Y.5
  • 3
    • 0033788756 scopus 로고    scopus 로고
    • Metal coordination and mechanism of multicopper nitrite reductase
    • S. Suzuki, K. Kataoka, and K. Yamaguchi Metal coordination and mechanism of multicopper nitrite reductase Acc. Chem. Res. 33 2000 728 735
    • (2000) Acc. Chem. Res. , vol.33 , pp. 728-735
    • Suzuki, S.1    Kataoka, K.2    Yamaguchi, K.3
  • 4
    • 8444245920 scopus 로고    scopus 로고
    • Characterization of two type 1 Cu sites of Hyphomicrobium denitrificans nitrite reductase: A new class of copper-containing nitrite reductases
    • K. Yamaguchi, K. Kataoka, M. Kobayashi, K. Itoh, A. Fukui, and S. Suzuki Characterization of two type 1 Cu sites of Hyphomicrobium denitrificans nitrite reductase: a new class of copper-containing nitrite reductases Biochemistry 43 2004 14180 14188
    • (2004) Biochemistry , vol.43 , pp. 14180-14188
    • Yamaguchi, K.1    Kataoka, K.2    Kobayashi, M.3    Itoh, K.4    Fukui, A.5    Suzuki, S.6
  • 5
    • 11244296214 scopus 로고    scopus 로고
    • Structure-based engineering of Alcaligenes xylosoxidans copper-containing nitrite reductase enhances intermolecular electron transfer reaction with pseudoazurin
    • K. Kataoka, K. Yamaguchi, M. Kobayashi, T. Mori, N. Bokui, and S. Suzuki Structure-based engineering of Alcaligenes xylosoxidans copper-containing nitrite reductase enhances intermolecular electron transfer reaction with pseudoazurin J. Biol. Chem. 279 2004 53374 53378
    • (2004) J. Biol. Chem. , vol.279 , pp. 53374-53378
    • Kataoka, K.1    Yamaguchi, K.2    Kobayashi, M.3    Mori, T.4    Bokui, N.5    Suzuki, S.6
  • 6
    • 0037418715 scopus 로고    scopus 로고
    • Characterization and function of Met150Gln mutant of copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013
    • K. Kataoka, K. Yamaguchi, S. Sakai, K. Takagi, and S. Suzuki Characterization and function of Met150Gln mutant of copper-containing nitrite reductase from Achromobacter cycloclastes IAM1013 Biochem. Biophys. Res. Commun. 303 2003 519 524
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 519-524
    • Kataoka, K.1    Yamaguchi, K.2    Sakai, S.3    Takagi, K.4    Suzuki, S.5
  • 7
    • 0036301145 scopus 로고    scopus 로고
    • Electron donation between copper containing nitrite reductases and cupredoxins: The nature of protein-protein interaction in complex formation
    • L.M. Murphy, F.E. Dodd, F.K. Yousafzai, R.R. Eady, and S.S. Hasnain Electron donation between copper containing nitrite reductases and cupredoxins: the nature of protein-protein interaction in complex formation J. Mol. Biol. 315 2002 859 871
    • (2002) J. Mol. Biol. , vol.315 , pp. 859-871
    • Murphy, L.M.1    Dodd, F.E.2    Yousafzai, F.K.3    Eady, R.R.4    Hasnain, S.S.5
  • 8
    • 11144298974 scopus 로고    scopus 로고
    • Insights into redox partner interactions and substrate binding in nitrite reductase from Alcaligenes xylosoxidans: Crystal structures of the Trp138His and His313Gln mutants
    • M.L. Barrett, R.L. Harris, S. Antonyuk, M.A. Hough, M.J. Ellis, G. Saweres, R.R. Eady, and S.S. Hasnain Insights into redox partner interactions and substrate binding in nitrite reductase from Alcaligenes xylosoxidans: crystal structures of the Trp138His and His313Gln mutants Biochemistry 43 2004 16311 16319
    • (2004) Biochemistry , vol.43 , pp. 16311-16319
    • Barrett, M.L.1    Harris, R.L.2    Antonyuk, S.3    Hough, M.A.4    Ellis, M.J.5    Saweres, G.6    Eady, R.R.7    Hasnain, S.S.8
  • 9
    • 0034097583 scopus 로고    scopus 로고
    • Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase
    • K. Kataoka, H. Furusawa, K. Takagi, K. Yamaguchi, and S. Suzuki Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase J. Biochem. 127 2000 345 350
    • (2000) J. Biochem. , vol.127 , pp. 345-350
    • Kataoka, K.1    Furusawa, H.2    Takagi, K.3    Yamaguchi, K.4    Suzuki, S.5
  • 11
    • 0030658026 scopus 로고    scopus 로고
    • Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis
    • M.E.P. Murphy, S. Yurley, and E.T. Adman Structure of nitrite bound to copper-containing nitrite reductase from Alcaligenes faecalis J. Biol. Chem. 272 1997 28455 28460
    • (1997) J. Biol. Chem. , vol.272 , pp. 28455-28460
    • Murphy, M.E.P.1    Yurley, S.2    Adman, E.T.3
  • 12
    • 0029794252 scopus 로고    scopus 로고
    • Electronic structure of the perturbed blue copper site in nitrite reductase: Spectroscopic properties, bonding, and implications for the entatic/rack state
    • L.B. LaCroix, S.E. Shadle, Y. Wang, B.A. Averill, B. Hedman, K.O. Hodgson, and E.I. Solomon Electronic structure of the perturbed blue copper site in nitrite reductase: spectroscopic properties, bonding, and implications for the entatic/rack state J. Am. Chem. Soc. 118 1996 7755 7768
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7755-7768
    • Lacroix, L.B.1    Shadle, S.E.2    Wang, Y.3    Averill, B.A.4    Hedman, B.5    Hodgson, K.O.6    Solomon, E.I.7
  • 14
    • 0032544483 scopus 로고    scopus 로고
    • X-ray structure of a blue-copper nitrite reductase in two crystal forms. the nature of the copper sites, mode of substrate binding and recognition by redox partner
    • F.E. Dodd, J. Van Beeumen, R.R. Eady, and S.S. Hasnain X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner J. Mol. Biol. 282 1998 369 382
    • (1998) J. Mol. Biol. , vol.282 , pp. 369-382
    • Dodd, F.E.1    Van Beeumen, J.2    Eady, R.R.3    Hasnain, S.S.4
  • 15
    • 0031786665 scopus 로고    scopus 로고
    • Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: A comparison between blue and green nitrite reductases
    • T. Inoue, M. Gotoda, Deligeer, K. Kataoka, S. Suzuki, K. Yamaguchi, H. Watanabe, M. Goho, and Y. Kai Type 1 Cu structure of blue nitrite reductase from Alcaligenes xylosoxidans GIFU 1051 at 2.05 Å resolution: a comparison between blue and green nitrite reductases J. Biochem. 124 1998 876 879
    • (1998) J. Biochem. , vol.124 , pp. 876-879
    • Inoue, T.1    Gotoda, M.2    Deligeer3    Kataoka, K.4    Suzuki, S.5    Yamaguchi, K.6    Watanabe, H.7    Goho, M.8    Kai, Y.9
  • 16
    • 0002621882 scopus 로고
    • Electrochemical properties of copper proteins, pseudoazurin, and nitrite reductase from Achromobacter cycloclastes IAM 1013
    • T. Kohzuma, S. Takase, S. Shidara, and S. Suzuki Electrochemical properties of copper proteins, pseudoazurin, and nitrite reductase from Achromobacter cycloclastes IAM 1013 Chem. Lett. 1993 149 152
    • (1993) Chem. Lett. , pp. 149-152
    • Kohzuma, T.1    Takase, S.2    Shidara, S.3    Suzuki, S.4
  • 17
    • 0040401549 scopus 로고
    • Theory of stationary electrode polarography, single scan and cyclic methods applied to reversible, irreversible, and kinetic systems
    • R.S. Nicholson, and I. Shain Theory of stationary electrode polarography, single scan and cyclic methods applied to reversible, irreversible, and kinetic systems Anal. Chem. 36 1964 706 723
    • (1964) Anal. Chem. , vol.36 , pp. 706-723
    • Nicholson, R.S.1    Shain, I.2
  • 18
    • 0019327137 scopus 로고
    • Direct demonstration of electron transfer between tryptophan and tyrosine in proteins
    • W.A. Pürtz, J. Butler, E.J. Land, and A.J. Swallow Direct demonstration of electron transfer between tryptophan and tyrosine in proteins Biochem. Biophys. Res. Commun. 96 1980 408 414
    • (1980) Biochem. Biophys. Res. Commun. , vol.96 , pp. 408-414
    • Pürtz, W.A.1    Butler, J.2    Land, E.J.3    Swallow, A.J.4
  • 20
    • 33845183951 scopus 로고
    • Long-range electron transfer between tyrosine and tryptophan in peptides
    • M. Faraggi, M.R. DeFelippis, and M.H. Klapper Long-range electron transfer between tyrosine and tryptophan in peptides J. Am. Chem. Soc. 111 1989 5141 5145
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5141-5145
    • Faraggi, M.1    Defelippis, M.R.2    Klapper, M.H.3
  • 21
    • 0026563022 scopus 로고
    • A possible biological role of the electron transfer between tyrosine and tryptophan
    • C.-Y. Lee A possible biological role of the electron transfer between tyrosine and tryptophan FEBS Lett. 299 1992 119 123
    • (1992) FEBS Lett. , vol.299 , pp. 119-123
    • Lee, C.-Y.1
  • 22
    • 0033545878 scopus 로고    scopus 로고
    • Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans
    • C. Aubert, P. Mathis, A.P.M. Eker, and K. Brettel Intraprotein electron transfer between tyrosine and tryptophan in DNA photolyase from Anacystis nidulans Proc. Natl. Acad. Sci. USA 96 1999 5423 5427
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5423-5427
    • Aubert, C.1    Mathis, P.2    Eker, A.P.M.3    Brettel, K.4
  • 23
    • 20644449681 scopus 로고    scopus 로고
    • Electron transfer between tryptophan and tyrosine: Theoretical calculation of electron transfer matrix element for intramolecular hole transfer
    • X.-Y. Li Electron transfer between tryptophan and tyrosine: theoretical calculation of electron transfer matrix element for intramolecular hole transfer J. Comp. Chem. 22 2001 565 579
    • (2001) J. Comp. Chem. , vol.22 , pp. 565-579
    • Li, X.-Y.1
  • 24
    • 0041322950 scopus 로고    scopus 로고
    • Re-evaluation of intramolecular long-range electron transfer between tyrosine and tryptophan in lysozymes: Evidence for the participation of other residues
    • M. Stuart-Audette, Y. Blouquit, M. Faraggi, C. Sicard-Roselli, C. Houee-Levin, and P. Jolles Re-evaluation of intramolecular long-range electron transfer between tyrosine and tryptophan in lysozymes: evidence for the participation of other residues Eur. J. Biochem. 270 2003 3565 3571
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3565-3571
    • Stuart-Audette, M.1    Blouquit, Y.2    Faraggi, M.3    Sicard-Roselli, C.4    Houee-Levin, C.5    Jolles, P.6
  • 25
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunneling in biological oxidation-reduction
    • C.C. Page, C.C. Moser, X. Chen, and P.L. Dutton Natural engineering principles of electron tunneling in biological oxidation-reduction Nature 402 1999 47 52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 26
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • C.C Page, C.C. Moser, and P.L. Dutton Mechanism for electron transfer within and between proteins Curr. Opin. Chem. Biol. 7 2003 551 556
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 551-556
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.