Structure of a dioxygen reduction enzyme from Desulfovibrio gigas.
作者： Maria A. Carrondo , Carlos Frazão , Gabriela Silva , Cláudio M. Gomes , Pedro Matias
DOI: 10.1038/80961
关键词: Flavodoxin 、 Oxidoreductase 、 Biology 、 Biochemistry 、 Rubredoxin 、 Monomer 、 Enzyme 、 Desulfovibrio gigas 、 Metabolic pathway 、 Oxygen
摘要: Desulfovibrio gigas is a strict anaerobe that contains well-characterized metabolic pathway enables it to survive transient contacts with oxygen. The terminal enzyme in this pathway, rubredoxin:oxygen oxidoreductase (ROO) reduces oxygen water direct and safe way. 2.5 A resolution crystal structure of ROO shows each monomer homodimeric consists novel combination two domains, flavodoxin-like domain Zn-β-lactamase-like di-iron center for dioxygen reduction. This the first member superfamily enzymes widespread facultative anaerobes, indicating its broad physiological significance.
rcsb.org
nature.com参考文章(29)
A. Carfi, S. Pares, E. Duée, M. Galleni, C. Duez, J. M. Frère, O. Dideberg, The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. The EMBO Journal. ,vol. 14, pp. 4914- 4921 ,(1995) , 10.1002/J.1460-2075.1995.TB00174.X
Zbyszek Otwinowski, Wladek Minor, Processing of X-ray diffraction data collected in oscillation mode Methods in Enzymology. ,vol. 276, pp. 307- 326 ,(1997) , 10.1016/S0076-6879(97)76066-X
P Fareleira, J Legall, A V Xavier, H Santos, Pathways for utilization of carbon reserves in Desulfovibrio gigas under fermentative and respiratory conditions. Journal of bacteriology. ,vol. 179, pp. 3972- 3980 ,(1997) , 10.1128/JB.179.12.3972-3980.1997
J. J. R. Fraústo da Silva, R. J. P. Williams, The Natural Selection of the Chemical Elements: The Environment and Life's Chemistry ,(1997)
Eric de La Fortelle, Gérard Bricogne, [27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods Methods in Enzymology. ,vol. 276, pp. 472- 494 ,(1997) , 10.1016/S0076-6879(97)76073-7
Wayne A. Hendrickson, Craig M. Ogata, [28] Phase determination from multiwavelength anomalous diffraction measurements. Methods in Enzymology. ,vol. 276, pp. 494- 523 ,(1997) , 10.1016/S0076-6879(97)76074-9
George M. Sheldrick, Thomas R. Schneider, SHELXL: high-resolution refinement. Methods in Enzymology. ,vol. 277, pp. 319- 343 ,(1997) , 10.1016/S0076-6879(97)77018-6
Cláudio M. Gomes, Gabriela Silva, Solange Oliveira, Jean LeGall, Ming-Yih Liu, António V. Xavier, Claudina Rodrigues-Pousada, Miguel Teixeira, Studies on the Redox Centers of the Terminal Oxidase fromDesulfovibrio gigas and Evidence for Its Interaction with Rubredoxin Journal of Biological Chemistry. ,vol. 272, pp. 22502- 22508 ,(1997) , 10.1074/JBC.272.36.22502
Alain Wasserfallen, Sandra Ragettli, Yves Jouanneau, Thomas Leisinger, A family of flavoproteins in the domains Archaea and Bacteria FEBS Journal. ,vol. 254, pp. 325- 332 ,(1998) , 10.1046/J.1432-1327.1998.2540325.X
E Osano, Y Arakawa, R Wacharotayankun, M Ohta, T Horii, H Ito, F Yoshimura, N Kato, Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrobial Agents and Chemotherapy. ,vol. 38, pp. 71- 78 ,(1994) , 10.1128/AAC.38.1.71