Proton translocation by bacteriorhodopsin and heme-copper oxidases

被引：128

作者：

Wikström, M

机构：

[1] Univ Helsinki, Inst Biomed Sci, Dept Med Chem, Helsinki Bioenerget Grp, FIN-00014 Helsinki, Finland

[2] Univ Helsinki, Inst Biomed Sci, Dept Med Chem, Bioctr Helsinki, FIN-00014 Helsinki, Finland

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1998年 / 8卷 / 04期

基金：

芬兰科学院;

关键词：

D O I：

10.1016/S0959-440X(98)80127-9

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 translocation is the means by which free energy is conserved from oxygen reduction by the respiratory heme-copper oxidases and from sunlight by bacteriorhodopsin, Three-dimensional structures at atomic resolution of both proteins have aided functional studies of the proton translocation mechanism. A comparison reveals common structural and functional features that may be unique to the primary proton pumps in biology.

引用

收藏

页码：480 / 488

页数：9

相关论文

共 69 条

[21]

Hofacker I, 1998, PROTEINS, V30, P100, DOI 10.1002/(SICI)1097-0134(199801)30:1<100::AID-PROT9>3.3.CO

[22]

2-Q

[23] MOLECULAR-DYNAMICS STUDY OF BACTERIORHODOPSIN AND ARTIFICIAL PIGMENTS [J].

HUMPHREY, W ;

LOGUNOV, I ;

SCHULTEN, K ;

SHEVES, M .

BIOCHEMISTRY, 1994, 33 (12) :3668-3678

[24] STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF CYTOCHROME-C-OXIDASE FROM PARACOCCUS-DENITRIFICANS [J].

IWATA, S ;

OSTERMEIER, C ;

LUDWIG, B ;

MICHEL, H .

NATURE, 1995, 376 (6542) :660-669

[25] Effects of mutation of the conserved lysine-362 in cytochrome c oxidase from Rhodobacter sphaeroides [J].

Junemann, S ;

Meunier, B ;

Gennis, RB ;

Rich, PR .

BIOCHEMISTRY, 1997, 36 (47) :14456-14464

[26] The coupling of electron transfer and proton translocation:: Electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase [J].

Kannt, A ;

Lancaster, CRD ;

Michel, H .

BIOPHYSICAL JOURNAL, 1998, 74 (02) :708-721

[27] Electron-proton interactions in terminal oxidases [J].

Karpefors, M ;

Ädelroth, P ;

Aagaard, A ;

Sigurdson, H ;

Ek, MS ;

Brzezinski, P .

BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1998, 1365 (1-2) :159-169

[28] Surface of bacteriorhodopsin revealed by high-resolution electron crystallography [J].

Kimura, Y ;

Vassylyev, DG ;

Miyazawa, A ;

Kidera, A ;

Matsushima, M ;

Mitsuoka, K ;

Murata, K ;

Hirai, T ;

Fujiyoshi, Y .

NATURE, 1997, 389 (6647) :206-211

[29] The roles of the two proton input channels in cytochrome c oxidase from Rhodobacter sphaeroides probed by the effects of site-directed mutations on time-resolved electrogenic intraprotein proton transfer [J].

Konstantinov, AA ;

Siletsky, S ;

Mitchell, D ;

Kaulen, A ;

Gennis, RB .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (17) :9085-9090

[30] The coupling of light-induced electron transfer and proton uptake as derived from crystal structures of reaction centres from Rhodopseudomonas viridis modified at the binding site of the secondary quinone, Q(B) [J].

Lancaster, CRD ;

Michel, H .

STRUCTURE, 1997, 5 (10) :1339-1359

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