The structure of Acidithiobacillus ferrooxidans c(4)-cytochrome: a model for complex-induced electron transfer tuning.
作者： Chantal Abergel , Wolfgang Nitschke , Guillaume Malarte , Mireille Bruschi , Jean-Michel Claverie
DOI: 10.1016/S0969-2126(03)00072-8
关键词: Redox 、 Rusticyanin 、 Copper protein 、 Inorganic chemistry 、 Electron paramagnetic resonance 、 Electron transfer 、 Cytochrome 、 Electron transport chain 、 Chemistry 、 Divalent 、 Stereochemistry
摘要: Abstract The study of electron transfer between the copper protein rusticyanin (RCy) and c 4 -cytochrome CYC 41 acidophilic bacterium Acidithiobacillus ferrooxidans has evidenced a remarkable decrease RCy's redox potential upon complex formation. structure obtained at 2.2 A resolution highlighted specific glutamate residue (E121) involved in zinc binding as potentially playing central role this effect, required for to occur. EPR stopped-flow experiments confirmed strong inhibitory effect divalent cations on :RCy docking analysis RCy allows us propose detailed model complex-induced tuning agreement with our experimental data, which could be representative other proteins transfer.
rcsb.org
elsevier.com参考文章(30)
Richard E. Dickerson, Russell Timkovich, 7 Cytochromes c The Enzymes. ,vol. 11, pp. 397- 547 ,(1975) , 10.1016/S1874-6047(08)60215-2
Graham W. Pettigrew, Geoffrey R. Moore, Geoffrey Moore, Cytochromes c: Evolutionary, Structural and Physicochemical Aspects ,(1990)
W.A. Hendrickson, J.R. Horton, D.M. LeMaster, Selenomethionyl proteins produced for analysis by multiwavelength anomalous diffraction (MAD) : a vehicle for direct determination of three-dimensional structure The EMBO Journal. ,vol. 9, pp. 1665- 1672 ,(1990) , 10.1002/J.1460-2075.1990.TB08287.X
Desmond G Higgins, Julie D Thompson, Toby J Gibson, USING CLUSTAL FOR MULTIPLE SEQUENCE ALIGNMENTS Methods in Enzymology. ,vol. 266, pp. 383- 402 ,(1996) , 10.1016/S0076-6879(96)66024-8
Bi-Cheng Wang, Resolution of phase ambiguity in macromolecular crystallography. Methods in Enzymology. ,vol. 115, pp. 90- 112 ,(1985) , 10.1016/0076-6879(85)15009-3
K A Gray, V L Davidson, D B Knaff, Complex formation between methylamine dehydrogenase and amicyanin from Paracoccus denitrificans. Journal of Biological Chemistry. ,vol. 263, pp. 13987- 13990 ,(1988) , 10.1016/S0021-9258(18)68173-6
David L. Turner, Determination of Haem Electronic Structure in His‐Met Cytochromes c by 13C‐NMR FEBS Journal. ,vol. 227, pp. 829- 837 ,(1995) , 10.1111/J.1432-1033.1995.0829P.X
Thomas C. Terwilliger, Joel Berendzen, Automated MAD and MIR structure solution Acta Crystallographica Section D-biological Crystallography. ,vol. 55, pp. 849- 861 ,(1999) , 10.1107/S0907444999000839
Zhenyu Zhu, Louise M. Cunane, Zhi-wei Chen, Rosemary C. E. Durley, F. Scott Mathews, Victor L. Davidson, MOLECULAR BASIS FOR INTERPROTEIN COMPLEX-DEPENDENT EFFECTS ON THE REDOX PROPERTIES OF AMICYANIN Biochemistry. ,vol. 37, pp. 17128- 17136 ,(1998) , 10.1021/BI9817919
Claude More, Val�rie Belle, Marcel Asso, Andr� Fournel, Guy Roger, Bruno Guigliarelli, Patrick Bertrand, EPR spectroscopy: a powerful technique for the structural and functional investigation of metalloproteins. Biospectroscopy. ,vol. 5, ,(1999) , 10.1002/(SICI)1520-6343(1999)5:5+<S3::AID-BSPY2>3.0.CO;2-P