메뉴 건너뛰기




Volumn 90, Issue 1, 2006, Pages 23-28

The atypical iron-coordination geometry of cytochrome f remains unchanged upon binding to plastocyanin, as inferred by XAS

Author keywords

Cytochrome f; Electron transfer; Metalloproteins; Plastocyanin; Transient complexes; X ray absorption spectroscopy

Indexed keywords

CYTOCHROME F; LIGAND; PLASTOCYANIN;

EID: 33846354173     PISSN: 01668595     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11120-006-9102-8     Document Type: Article
Times cited : (6)

References (26)
  • 1
    • 23944504726 scopus 로고    scopus 로고
    • Laser flash-induced kinetic analysis of cytochrome f oxidation by wild-type and mutant plastocyanin from the cyanobacterium Nostoc sp PCC 7119
    • Albarrán C, Navarro JA, Molina-Heredia FP, Murdoch PS, De la Rosa MA, Hervás M (2005) Laser flash-induced kinetic analysis of cytochrome f oxidation by wild-type and mutant plastocyanin from the cyanobacterium Nostoc sp PCC 7119. Biochemistry 44:11601-11607
    • (2005) Biochemistry , vol.44 , pp. 11601-11607
    • Albarrán, C.1    Navarro, J.A.2    Molina-Heredia, F.P.3    Murdoch, P.S.4    De la Rosa, M.A.5    Hervás, M.6
  • 2
    • 1542321529 scopus 로고    scopus 로고
    • 6f: Structure for signalling and vectorial metabolism
    • 6f: structure for signalling and vectorial metabolism. Trends Plant Sci 9:130-137
    • (2004) Trends Plant Sci , vol.9 , pp. 130-137
    • Allen, J.F.1
  • 3
    • 0033609516 scopus 로고    scopus 로고
    • Structure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum
    • Carrel CJ, Schlarb BG, Bendall DS, Howe CJ, Cramer WA, Smith JL (1999) Structure of the soluble domain of cytochrome f from the cyanobacterium Phormidium laminosum. Biochemistry 38:9590-9599
    • (1999) Biochemistry , vol.38 , pp. 9590-9599
    • Carrel, C.J.1    Schlarb, B.G.2    Bendall, D.S.3    Howe, C.J.4    Cramer, W.A.5    Smith, J.L.6
  • 4
    • 0013253713 scopus 로고    scopus 로고
    • Determination of iron-ligand bond lengths in ferric and ferrous horse heart cytochrome c using multiple-scattering analyses of XAFS data
    • Cheng MG, Rich AM, Armstrong RS, Ellis PJ, Lay PA (1999) Determination of iron-ligand bond lengths in ferric and ferrous horse heart cytochrome c using multiple-scattering analyses of XAFS data. Inorg Chem 38:5703-5708
    • (1999) Inorg Chem , vol.38 , pp. 5703-5708
    • Cheng, M.G.1    Rich, A.M.2    Armstrong, R.S.3    Ellis, P.J.4    Lay, P.A.5
  • 6
    • 21444446549 scopus 로고    scopus 로고
    • The orientation of plastocyanin in the complex with cytochrome f from the cyanobacterium Nostoc determined by paramagnetic NMR
    • Díaz-Moreno I, Díaz-Quintana A, De la Rosa MA, Ubbink M (2005a) The orientation of plastocyanin in the complex with cytochrome f from the cyanobacterium Nostoc determined by paramagnetic NMR. J Biol Chem 280:18908-18915
    • (2005) J Biol Chem , vol.280 , pp. 18908-18915
    • Díaz-Moreno, I.1    Díaz-Quintana, A.2    De la Rosa, M.A.3    Ubbink, M.4
  • 10
    • 2942589291 scopus 로고    scopus 로고
    • The linked conservation of structure and function in a family of high diversity: The monomeric cupredoxins
    • Gough J, Chotia C (2004) The linked conservation of structure and function in a family of high diversity: The monomeric cupredoxins. Structure 12:917-925
    • (2004) Structure , vol.12 , pp. 917-925
    • Gough, J.1    Chotia, C.2
  • 11
    • 0000121207 scopus 로고
    • Cytochrome f: Structure, function and biosynthesis
    • Gray JC (1992) Cytochrome f: structure, function and biosynthesis. Photosynth Res 34:359-374
    • (1992) Photosynth Res , vol.34 , pp. 359-374
    • Gray, J.C.1
  • 12
    • 0142151125 scopus 로고    scopus 로고
    • Electron Transfer between Membrane Complexes and Soluble Proteins in Photosynthesis
    • Hervás M, Navarro JA, De la Rosa MA (2003) Electron Transfer between Membrane Complexes and Soluble Proteins in Photosynthesis. Acc Chem Res 36:798-805
    • (2003) Acc Chem Res , vol.36 , pp. 798-805
    • Hervás, M.1    Navarro, J.A.2    De la Rosa, M.A.3
  • 13
    • 0034598395 scopus 로고    scopus 로고
    • Electron transfers amongst cytochrome f, plastocyanin and photosystem I: Kinetics and mechanisms
    • Hope AB (2000) Electron transfers amongst cytochrome f, plastocyanin and photosystem I: Kinetics and mechanisms. Biochim Biophys Acta 1456:5-26
    • (2000) Biochim Biophys Acta , vol.1456 , pp. 5-26
    • Hope, A.B.1
  • 14
    • 18044367301 scopus 로고    scopus 로고
    • The transient interaction of poplar plastocyanin with cytochrome f studied by 2D-NMR spectroscopy: Effects of ionic strength and pH
    • Lange C, Cornvik T, Díaz-Moreno I, Ubbink M (2005) The transient interaction of poplar plastocyanin with cytochrome f studied by 2D-NMR spectroscopy: effects of ionic strength and pH. BBA Bioenergetics 1707:179-188
    • (2005) BBA Bioenergetics , vol.1707 , pp. 179-188
    • Lange, C.1    Cornvik, T.2    Díaz-Moreno, I.3    Ubbink, M.4
  • 15
    • 0028773015 scopus 로고
    • Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation
    • Martinez SE, Huang M, Szczpaniak A, Cramer WA, Smith JL (1994) Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. Structure 2:95-105
    • (1994) Structure , vol.2 , pp. 95-105
    • Martinez, S.E.1    Huang, M.2    Szczpaniak, A.3    Cramer, W.A.4    Smith, J.L.5
  • 17
    • 21444431710 scopus 로고    scopus 로고
    • Structure of the intermolecular complex between plastocyanin and cytochrome f from spinach
    • Musiani F, Dikiy A, Semenov AY, Ciurli S (2005) Structure of the intermolecular complex between plastocyanin and cytochrome f from spinach. J Biol Chem 280:18883-18841
    • (2005) J Biol Chem , vol.280 , pp. 18883-18841
    • Musiani, F.1    Dikiy, A.2    Semenov, A.Y.3    Ciurli, S.4
  • 18
    • 54749090787 scopus 로고
    • Analysis of multiple-scattering XAFS data using theoretical standards
    • Newville M, Ravel B, Haskel D, Rehr JJ, Stern EA, Yacoby Y (1995) Analysis of multiple-scattering XAFS data using theoretical standards. Physica B 208-209:154-155
    • (1995) Physica B , vol.208-209 , pp. 154-155
    • Newville, M.1    Ravel, B.2    Haskel, D.3    Rehr, J.J.4    Stern, E.A.5    Yacoby, Y.6
  • 20
    • 11844260365 scopus 로고
    • High-order multiple scattering calculations of x-ray-absorption fine structure
    • Rehr JJ, Zabinsky SI, Albers RC (1992) High-order multiple scattering calculations of x-ray-absorption fine structure. Phys Rev Let 69:3397-3401
    • (1992) Phys Rev Let , vol.69 , pp. 3397-3401
    • Rehr, J.J.1    Zabinsky, S.I.2    Albers, R.C.3
  • 21
    • 0020516949 scopus 로고
    • Distribution of plastocyanin and soluble plastidic cytochrome c in various classes of algae
    • Sandman G, Reck H, Kessler E, Böger P (1983) Distribution of plastocyanin and soluble plastidic cytochrome c in various classes of algae. Arch Microbiol 134:23-27
    • (1983) Arch Microbiol , vol.134 , pp. 23-27
    • Sandman, G.1    Reck, H.2    Kessler, E.3    Böger, P.4
  • 23
    • 0016957826 scopus 로고
    • Observation and interpretation of X-ray absorption edges in iron compounds and proteins
    • Shulman RG, Yafet T, Eisenberger P, Blumberg WE (1976) Observation and interpretation of X-ray absorption edges in iron compounds and proteins. Proc Natl Acad Sci USA 73:1384-1388
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 1384-1388
    • Shulman, R.G.1    Yafet, T.2    Eisenberger, P.3    Blumberg, W.E.4
  • 24
    • 37049098774 scopus 로고
    • Tilden Lecture: Structure and Electron-transfer Reactivity of the Blue Copper Protein Plastocyanin
    • Sykes AG (1985) Tilden Lecture: Structure and Electron-transfer Reactivity of the Blue Copper Protein Plastocyanin. Chem Soc Rev 14:283-315
    • (1985) Chem Soc Rev , vol.14 , pp. 283-315
    • Sykes, A.G.1
  • 25
    • 4043055221 scopus 로고    scopus 로고
    • Complexes of photosynthetic redox proteins studied by NMR
    • Ubbink M (2004) Complexes of photosynthetic redox proteins studied by NMR. Phosynth Res 81:277-287
    • (2004) Phosynth Res , vol.81 , pp. 277-287
    • Ubbink, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.