The transmembrane domain and the proton channel in proton-pumping transhydrogenases

被引:16
作者
Bizouarn, T [1 ]
Meuller, J [1 ]
Axelsson, M [1 ]
Rydström, J [1 ]
机构
[1] Gothenburg Univ, Dept Biochem & Biophys, S-41390 Gothenburg, Sweden
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2000年 / 1459卷 / 2-3期
关键词
transhydrogenase; proton pump; membrane protein; nicotinamide nucleotide; nicotinamide adenine dinucleotide; nicotinamide adenine dinucleotide phosphate;
D O I
10.1016/S0005-2728(00)00163-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Proton-pumping nicotinamide nucleotide transhydrogenases are composed of three main domains, the NAD(H)-binding and NADP(H)-binding hydrophilic domains I (dI) and III (dIII), respectively, and the hydrophobic domain II (dII) containing the assumed proton channel, dII in the Escherichia coli enzyme has recently been characterised with regard to topology and a packing model of the helix bundle in dII is proposed. Extensive mutagenesis of conserved charged residues of this domain showed that important residues are beta His91 and beta Asn222. The pH dependence of beta H91D, as well as beta T91C (unpublished), when compared to that of wild type shows that reduction of 3-acetylpyridine-NAD(+) by NADPH, i.e., the reverse reaction, is optimal at a pH essentially coinciding with the pk(a) of the residue in the beta 91 position. It is therefore concluded that the wild-type transhydrogenase is regulated by the degree of protonation of beta His91. The mechanisms of the interactions between dI+dIII and dII are suggested to involve pronounced conformational changes in a 'hinge' region around beta R265. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:284 / 290
页数:7
相关论文
共 32 条
[1]  
AHMAD S, 1992, J BIOL CHEM, V267, P7007
[2]   Proton translocating nicotinamide nucleotide transhydrogenase from E-coli.: Mechanism of action deduced from its structural and catalytic properties [J].
Bizouarn, T ;
Fjellström, O ;
Meuller, J ;
Axelsson, M ;
Bergkvist, A ;
Johansson, C ;
Karlsson, BG ;
Rydström, J .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2000, 1457 (03) :211-228
[3]  
BIZOUARN T, 2000, IN PRESS EUR J BIOCH
[4]   Mutation of conserved polar residues in the transmembrane domain of the proton-pumping pyridine nucleotide transhydrogenase of Escherichia coli [J].
Bragg, PD ;
Hou, C .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 363 (01) :182-190
[5]   NUCLEOTIDE-SEQUENCE OF THE PNTA AND PNTB GENES ENCODING THE PYRIDINE-NUCLEOTIDE TRANSHYDROGENASE OF ESCHERICHIA-COLI [J].
CLARKE, DM ;
LOO, TW ;
GILLAM, S ;
BRAGG, PD .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1986, 158 (03) :647-653
[6]   PROPERTIES OF THE SOLUBLE POLYPEPTIDE OF THE PROTON-TRANSLOCATING TRANSHYDROGENASE FROM RHODOSPIRILLUM-RUBRUM OBTAINED BY EXPRESSION IN ESCHERICHIA-COLI [J].
DIGGLE, C ;
HUTTON, M ;
JONES, GR ;
THOMAS, CM ;
JACKSON, JB .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1995, 228 (03) :719-726
[7]   Properties of the purified, recombinant, NADP(H)-binding domain III of the proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum [J].
Diggle, C ;
Bizouarn, T ;
Cotton, NPJ ;
Jackson, JB .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1996, 241 (01) :162-170
[8]   Catalytic properties of hybrid complexes of the NAD(H)-binding and NADP(H)-binding domains of the proton-translocating transhydrogenases from Escherichia coli and Rhodospirillum rubrum [J].
Fjellström, O ;
Bizouarn, T ;
Zhang, JW ;
Rydström, J .
BIOCHEMISTRY, 1999, 38 (01) :415-422
[9]   Structural and catalytic properties of the expressed and purified NAD(H)- and NADP(H)-binding domains of proton-pumping transhydrogenase from Escherichia coli [J].
Fjellstrom, O ;
Johansson, C ;
Rydstrom, J .
BIOCHEMISTRY, 1997, 36 (38) :11331-11341
[10]   THE MECHANISM OF HYDRIDE TRANSFER BETWEEN NADH AND 3-ACETYLPYRIDINE ADENINE-DINUCLEOTIDE BY THE PYRIDINE-NUCLEOTIDE TRANSHYDROGENASE OF ESCHERICHIA-COLI [J].
GLAVAS, NA ;
BRAGG, PD .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1995, 1231 (03) :297-303