메뉴 건너뛰기




Volumn 16, Issue 8, 2011, Pages 1241-1254

The electron transfer complex between nitrous oxide reductase and its electron donors

Author keywords

Docking; Electron transfer complexes; Electron transfer pathway; Nitrous oxide reductase; Recognition

Indexed keywords

ALANINE; ASPARTIC ACID; COPPER PROTEIN; CYTOCHROME C; HEME; HEME C TYPE; HISTIDINE; LEUCINE; NITROUS OXIDE REDUCTASE; UNCLASSIFIED DRUG; VALINE;

EID: 84655163875     PISSN: 09498257     EISSN: 14321327     Source Type: Journal    
DOI: 10.1007/s00775-011-0812-9     Document Type: Article
Times cited : (27)

References (60)
  • 1
    • 0031456471 scopus 로고    scopus 로고
    • 9409151 1:CAS:528:DyaK2sXotVymtr8%3D
    • WG Zumft 1997 Microbiol Mol Biol Rev 61 533 616 9409151 1:CAS:528:DyaK2sXotVymtr8%3D
    • (1997) Microbiol Mol Biol Rev , vol.61 , pp. 533-616
    • Zumft, W.G.1
  • 2
    • 33750959735 scopus 로고    scopus 로고
    • Metalloenzymes of the denitrification pathway
    • DOI 10.1016/j.jinorgbio.2006.09.003, PII S0162013406002534
    • P Tavares AS Pereira JJG Moura I Moura 2006 J Inorg Biochem 100 2087 2100 17070915 10.1016/j.jinorgbio.2006.09.003 1:CAS:528:DC%2BD28Xht1Cgs7vF (Pubitemid 44738047)
    • (2006) Journal of Inorganic Biochemistry , vol.100 , Issue.12 , pp. 2087-2100
    • Tavares, P.1    Pereira, A.S.2    Moura, J.J.G.3    Moura, I.4
  • 3
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • DOI 10.1006/jmbi.1998.2439
    • L Lo Conte C Chothia J Janin 1999 J Mol Biol 285 2177 2198 9925793 10.1006/jmbi.1998.2439 (Pubitemid 29078179)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 4
    • 8444232122 scopus 로고    scopus 로고
    • Transient complexes of redox proteins: Structural and dynamic details from NMR studies
    • DOI 10.1002/jmr.686
    • M Prudencio M Ubbink 2004 J Mol Recognit 17 524 539 15386621 10.1002/jmr.686 1:CAS:528:DC%2BD2cXpvFOku7s%3D (Pubitemid 39484220)
    • (2004) Journal of Molecular Recognition , vol.17 , Issue.6 , pp. 524-539
    • Prudencio, M.1    Ubbink, M.2
  • 7
    • 0034212826 scopus 로고    scopus 로고
    • 10813819 10.1002/(SICI)1097-0134(20000601)39:4<372::AID-PROT100>3. 0.CO;2-Q 1:CAS:528:DC%2BD3cXjslChsLw%3D
    • PN Palma L Krippahl JE Wampler JJG Moura 2000 Proteins 39 372 384 10813819 10.1002/(SICI)1097-0134(20000601)39:4<372::AID-PROT100>3.0.CO;2-Q 1:CAS:528:DC%2BD3cXjslChsLw%3D
    • (2000) Proteins , vol.39 , pp. 372-384
    • Palma, P.N.1    Krippahl, L.2    Wampler, J.E.3    Moura, J.J.G.4
  • 10
    • 69249206552 scopus 로고    scopus 로고
    • 19651443 10.1016/j.jinorgbio.2009.07.006 1:CAS:528:DC%2BD1MXhtVKkt7rK
    • RM Almeida SR Pauleta I Moura JJG Moura 2009 J Inorg Biochem 103 1245 1253 19651443 10.1016/j.jinorgbio.2009.07.006 1:CAS:528:DC%2BD1MXhtVKkt7rK
    • (2009) J Inorg Biochem , vol.103 , pp. 1245-1253
    • Almeida, R.M.1    Pauleta, S.R.2    Moura, I.3    Moura, J.J.G.4
  • 11
    • 33749337025 scopus 로고    scopus 로고
    • 17027372 10.1016/S0065-2911(06)52003-X 1:CAS:528:DC%2BD1cXhvVChsr0%3D
    • WG Zumft PM Kroneck 2007 Adv Microb Physiol 52 107 227 17027372 10.1016/S0065-2911(06)52003-X 1:CAS:528:DC%2BD1cXhvVChsr0%3D
    • (2007) Adv Microb Physiol , vol.52 , pp. 107-227
    • Zumft, W.G.1    Kroneck, P.M.2
  • 15
    • 0034026215 scopus 로고    scopus 로고
    • Electron tunneling pathways in proteins
    • DOI 10.1016/S1367-5931(99)00074-5
    • JR Winkler 2000 Curr Opin Chem Biol 4 192 198 10742192 10.1016/S1367-5931(99)00074-5 1:CAS:528:DC%2BD3cXisVaiu7g%3D (Pubitemid 30189311)
    • (2000) Current Opinion in Chemical Biology , vol.4 , Issue.2 , pp. 192-198
    • Winkler, J.R.J.R.1
  • 16
    • 0032570589 scopus 로고    scopus 로고
    • Tryptophan 121 of subunit II is the electron entry site to cytochrome-c oxidase in Paracoccus denitrificans: Involvement of a hydrophobic patch in the docking reaction
    • DOI 10.1074/jbc.273.9.5132
    • H Witt F Malatesta F Nicoletti M Brunori B Ludwig 1998 J Biol Chem 273 5132 5136 9478966 10.1074/jbc.273.9.5132 1:CAS:528:DyaK1cXhs1Cntrk%3D (Pubitemid 28108674)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.9 , pp. 5132-5136
    • Witt, H.1    Malatesta, F.2    Nicoletti, F.3    Brunori, M.4    Ludwig, B.5
  • 17
    • 0344875555 scopus 로고    scopus 로고
    • A Fragments with Their Substrates
    • DOI 10.1074/jbc.M307594200
    • O Maneg B Ludwig F Malatesta 2003 J Biol Chem 278 46734 46740 12937163 10.1074/jbc.M307594200 1:CAS:528:DC%2BD3sXovFKks7g%3D (Pubitemid 37452252)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46734-46740
    • Maneg, O.1    Ludwig, B.2    Malatesta, F.3
  • 19
    • 0027476458 scopus 로고
    • 8383047 10.1111/j.1432-1033.1993.tb17683.x 1:CAS:528:DyaK3sXhvVKmsLw%3D
    • BC Berks D Baratta J Richardson SJ Ferguson 1993 Eur J Biochem 212 467 476 8383047 10.1111/j.1432-1033.1993.tb17683.x 1:CAS:528:DyaK3sXhvVKmsLw%3D
    • (1993) Eur J Biochem , vol.212 , pp. 467-476
    • Berks, B.C.1    Baratta, D.2    Richardson, J.3    Ferguson, S.J.4
  • 20
    • 0028345479 scopus 로고
    • 10.1099/13500872-140-2-389 1:CAS:528:DyaK2cXis1Gnu7Y%3D
    • JWB Moir SJ Ferguson 1994 Microbiology 140 389 397 10.1099/13500872-140- 2-389 1:CAS:528:DyaK2cXis1Gnu7Y%3D
    • (1994) Microbiology , vol.140 , pp. 389-397
    • Moir, J.W.B.1    Ferguson, S.J.2
  • 23
    • 18844413338 scopus 로고    scopus 로고
    • How does nitrous oxide reductase interact with its electron donors? A docking study
    • DOI 10.1002/prot.20437
    • K Mattila T Haltia 2005 Proteins 59 708 722 15822112 10.1002/prot.20437 1:CAS:528:DC%2BD2MXksVKmtL8%3D (Pubitemid 40695847)
    • (2005) Proteins: Structure, Function and Genetics , vol.59 , Issue.4 , pp. 708-722
    • Mattila, K.1    Haltia, T.2
  • 26
    • 35348827900 scopus 로고    scopus 로고
    • Anaerobic purification, characterization and preliminary mechanistic study of recombinant nitrous oxide reductase from Achromobacter cycloclastes
    • DOI 10.1016/j.jinorgbio.2007.06.029, PII S0162013407001444
    • K Fujita JM Chan JA Bollinger ML Alvarez DM Dooley 2007 J Inorg Biochem 101 1836 1844 17681606 10.1016/j.jinorgbio.2007.06.029 1:CAS:528: DC%2BD2sXhtF2itb3O (Pubitemid 47576198)
    • (2007) Journal of Inorganic Biochemistry , vol.101 , Issue.11-12 , pp. 1836-1844
    • Fujita, K.1    Chan, J.M.2    Bollinger, J.A.3    Alvarez, M.L.4    Dooley, D.M.5
  • 27
    • 0024961689 scopus 로고
    • 2536696 1:CAS:528:DyaL1MXhtlWjs7o%3D
    • S Teraguchi TC Hollocher 1989 J Biol Chem 264 1972 1979 2536696 1:CAS:528:DyaL1MXhtlWjs7o%3D
    • (1989) J Biol Chem , vol.264 , pp. 1972-1979
    • Teraguchi, S.1    Hollocher, T.C.2
  • 28
    • 0027273523 scopus 로고
    • The reaction of reduced cytochromes c with nitrous oxide reductase of Wolinella succinogenes
    • DOI 10.1016/0005-2728(93)90153-7
    • CS Zhang TC Hollocher 1993 Biochim Biophys Acta 1142 253 261 10.1016/0005-2728(93)90153-7 1:CAS:528:DyaK3sXkt1ensrY%3D (Pubitemid 23134652)
    • (1993) Biochimica et Biophysica Acta - Bioenergetics , vol.1142 , Issue.3 , pp. 253-261
    • Zhang, C.1    Hollocher, T.C.2
  • 30
    • 0028337124 scopus 로고
    • 8179333 10.1006/abbi.1994.1193 1:CAS:528:DyaK2cXkslKnsb8%3D
    • MM Benning TE Meyer HM Holden 1994 Arch Biochem Biophys 310 460 466 8179333 10.1006/abbi.1994.1193 1:CAS:528:DyaK2cXkslKnsb8%3D
    • (1994) Arch Biochem Biophys , vol.310 , pp. 460-466
    • Benning, M.M.1    Meyer, T.E.2    Holden, H.M.3
  • 32
    • 0033580855 scopus 로고    scopus 로고
    • Crystal structure determinations of oxidized and reduced pseudoazurins from Achromobacter cycloclastes: Concerted movement of copper site in redox forms with the rearrangement of hydrogen bond at a remote histidine
    • DOI 10.1074/jbc.274.25.17845
    • T Inoue N Nishio S Suzuki K Kataoka T Kohzuma Y Kai 1999 J Biol Chem 274 17845 17852 10364229 10.1074/jbc.274.25.17845 1:CAS:528:DyaK1MXktVyls7c%3D (Pubitemid 29283306)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.25 , pp. 17845-17852
    • Inoue, T.1    Nishio, N.2    Suzuki, S.3    Kataoka, K.4    Kohzuma, T.5    Kai, Y.6
  • 33
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • DOI 10.1016/0022-2836(90)90200-6
    • GW Bushnell GV Louie GD Brayer 1990 J Mol Biol 214 585 595 2166170 10.1016/0022-2836(90)90200-6 1:CAS:528:DyaK3cXlvVKku7s%3D (Pubitemid 20261984)
    • (1990) Journal of Molecular Biology , vol.214 , Issue.2 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 34
    • 37349082255 scopus 로고    scopus 로고
    • High resolution X-ray crystallographic structure of bovine heart cytochrome c and its application to the design of an electron transfer biosensor
    • DOI 10.1002/prot.21452
    • N Mirkin J Jaconcic V Stojanoff A Moreno 2008 Proteins 70 83 92 17634981 10.1002/prot.21452 1:CAS:528:DC%2BD1cXisVamug%3D%3D (Pubitemid 350293451)
    • (2008) Proteins: Structure, Function and Genetics , vol.70 , Issue.1 , pp. 83-92
    • Mirkin, N.1    Jaconcic, J.2    Stojanoff, V.3    Moreno, A.4
  • 36
    • 0003058940 scopus 로고
    • 10.1021/ja00037a004 1:CAS:528:DyaK38XitlWhtL0%3D
    • JN Betts DN Beratan JN Onuchic 1992 J Am Chem Soc 114 4043 4046 10.1021/ja00037a004 1:CAS:528:DyaK38XitlWhtL0%3D
    • (1992) J Am Chem Soc , vol.114 , pp. 4043-4046
    • Betts, J.N.1    Beratan, D.N.2    Onuchic, J.N.3
  • 39
    • 0027968068 scopus 로고
    • 7984417 10.1093/nar/22.22.4673 1:CAS:528:DyaK2MXitlSgu74%3D
    • JD Thompson DG Higgins TJ Gibson 1994 Nucleic Acids Res 22 4673 4680 7984417 10.1093/nar/22.22.4673 1:CAS:528:DyaK2MXitlSgu74%3D
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 41
    • 63849246525 scopus 로고    scopus 로고
    • 19247286 10.1038/nprot.2009.2 1:CAS:528:DC%2BD1MXivF2itbs%3D
    • LA Kelley MJ Sternberg 2009 Nat Protoc 4 363 371 19247286 10.1038/nprot.2009.2 1:CAS:528:DC%2BD1MXivF2itbs%3D
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 47
    • 0027056273 scopus 로고
    • 1334573 10.1126/science.1334573 1:CAS:528:DyaK3sXjsFWitg%3D%3D
    • H Pelletier J Kraut 1992 Science 258 1748 1755 1334573 10.1126/science.1334573 1:CAS:528:DyaK3sXjsFWitg%3D%3D
    • (1992) Science , vol.258 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 51
    • 0029995615 scopus 로고    scopus 로고
    • Studies on protein-protein interaction between copper-containing nitrite reductase and pseudoazurin from Alcaligenes faecalis S-6
    • DOI 10.1074/jbc.271.23.13680
    • M Kukimoto M Nishiyama M Tanokura ET Adman S Horinouchi 1996 J Biol Chem 271 13680 13683 8662745 10.1074/jbc.271.23.13680 1:CAS:528:DyaK28XjsVKqu7c%3D (Pubitemid 26187980)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.23 , pp. 13680-13683
    • Kukimoto, M.1    Nishiyama, M.2    Tanokura, M.3    Adman, E.T.4    Horinouchi, S.5
  • 52
    • 11244296214 scopus 로고    scopus 로고
    • Structure-based engineering of Alcaligenes xylosoxidans copper-containing nitrite reductase enhances intermolecular electron transfer reaction with pseudoazurin
    • DOI 10.1074/jbc.M410198200
    • K Kataoka K Yamaguchi M Kobayashi T Mori N Bokui S Suzuki 2004 J Biol Chem 279 53374 53378 15475344 10.1074/jbc.M410198200 1:CAS:528: DC%2BD2cXhtVKqurfF (Pubitemid 40063545)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.51 , pp. 53374-53378
    • Kataoka, K.1    Yamaguchi, K.2    Kobayashi, M.3    Mori, T.4    Bokui, N.5    Suzuki, S.6
  • 56
    • 0037133032 scopus 로고    scopus 로고
    • A site in cytochrome c oxidase of Rhodobacter sphaeroides: II. Rapid kinetic analysis of electron transfer
    • DOI 10.1021/bi0114630
    • K Wang L Geren Y Zhen L Ma S Ferguson-Miller B Durham F Millett 2002 Biochemistry 41 2298 2304 11841222 10.1021/bi0114630 1:CAS:528: DC%2BD38XmsVCqtg%3D%3D (Pubitemid 34160891)
    • (2002) Biochemistry , vol.41 , Issue.7 , pp. 2298-2304
    • Wang, K.1    Geren, L.2    Zhen, Y.3    Ma, L.4    Ferguson-Miller, S.5    Durham, B.6    Millett, F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.