Molecular basis of proton motive force generation:: Structure of formate dehydrogenase-N

被引:389
作者
Jormakka, M
Törnroth, S
Byrne, B
Iwata, S [1 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, Div Biomed Sci, London SW7 2AZ, England
[2] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AZ, England
[3] Univ Uppsala, BMC, Dept Biochem, S-75123 Uppsala, Sweden
关键词
D O I
10.1126/science.1068186
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The structure of the membrane protein formate dehydrogenase-N (Fdn-N), a major component of Escherichia coli nitrate respiration, has been determined at 1.6 angstroms. The structure demonstrates 11 redox centers, including molybdopterin-guanine dinucleotides, five [4Fe-4S] clusters, two heme b groups, and a menaquinone analog. These redox centers are aligned in a single chain, which extends almost 90 angstroms through the enzyme. The menaquinone reduction site associated with a possible proton pathway was also characterized. This structure provides critical insights into the proton motive force generation by redox loop, a common mechanism among a wide range of respiratory enzymes.
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页码:1863 / 1868
页数:6
相关论文
共 28 条
[1]   Topological analysis of the aerobic membrane-bound formate dehydrogenase of Escherichia coli [J].
Benoit, S ;
Abaibou, H ;
Mandrand-Berthelot, MA .
JOURNAL OF BACTERIOLOGY, 1998, 180 (24) :6625-6634
[2]  
BERG BL, 1991, J BIOL CHEM, V266, P22380
[3]   SEQUENCE-ANALYSIS OF SUBUNITS OF THE MEMBRANE-BOUND NITRATE REDUCTASE FROM A DENITRIFYING BACTERIUM - THE INTEGRAL MEMBRANE SUBUNIT PROVIDES A PROTOTYPE FOR THE DIHEME ELECTRON-CARRYING ARM OF A REDOX LOOP [J].
BERKS, BC ;
PAGE, MD ;
RICHARDSON, DJ ;
REILLY, A ;
CAVILL, A ;
OUTEN, F ;
FERGUSON, SJ .
MOLECULAR MICROBIOLOGY, 1995, 15 (02) :319-331
[4]   Enzymes and associated electron transport systems that catalyse the respiratory reduction of nitrogen oxides and oxyanions [J].
Berks, BC ;
Ferguson, SJ ;
Moir, JWB ;
Richardson, DJ .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1995, 1232 (03) :97-173
[5]  
BIEL S, IN PRESS EUR J BIOCH
[6]   The coordination and function of the redox centres of the membrane-bound nitrate reductases [J].
Blasco, F ;
Guigliarelli, B ;
Magalon, A ;
Asso, M ;
Giordano, G ;
Rothery, RA .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2001, 58 (02) :179-193
[7]   Crystal structure of formate dehydrogenase H: Catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster [J].
Boyington, JC ;
Gladyshev, VN ;
Khangulov, SV ;
Stadtman, TC ;
Sun, PD .
SCIENCE, 1997, 275 (5304) :1305-1308
[8]   Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods [J].
Dias, JM ;
Than, ME ;
Humm, A ;
Huber, R ;
Bourenkov, GP ;
Bartunik, HD ;
Bursakov, S ;
Calvete, J ;
Caldeira, J ;
Carneiro, C ;
Moura, JJG ;
Moura, I ;
Romao, MJ .
STRUCTURE, 1999, 7 (01) :65-79
[9]  
ESNOUF RM, 1997, J MOL GRAPHICS, V15, P133
[10]   Identification of histidine residues in Wolinella succinogenes hydrogenase that are essential for menaquinone reduction by H2 [J].
Gross, R ;
Simon, J ;
Lancaster, CRD ;
Kröger, A .
MOLECULAR MICROBIOLOGY, 1998, 30 (03) :639-646