Proton transport mechanism of bacteriorhodopsin as revealed by site-specific mutagenesis and protein sequence variability

被引:27
作者
Brown, LS [1 ]
机构
[1] Univ Calif Irvine, Dept Physiol & Biophys, Irvine, CA 92697 USA
关键词
bacteriorhodopsin; halobacteria; mutations; photocycle; proton transport; conserved residues;
D O I
10.1023/A:1013131318620
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
A large share of the current ideas about the mechanism of proton transport by bacteriorhodopsin has emerged from studies of site-specific mutants. This review is an attempt to check some of these ideas against the natural variability in the primary structure of the protein.
引用
收藏
页码:1249 / 1255
页数:7
相关论文
共 76 条
[1]   SUBSTITUTION OF AMINO-ACIDS IN HELIX-F OF BACTERIORHODOPSIN - EFFECTS ON THE PHOTOCHEMICAL CYCLE [J].
AHL, PL ;
STERN, LJ ;
MOGI, T ;
KHORANA, HG ;
ROTSCHILD, KJ .
BIOCHEMISTRY, 1989, 28 (26) :10028-10034
[2]   Evidence for long range allosteric interactions between the extracellular and cytoplasmic parts of bacteriorhodopsin from the mutant R82A and its second site revertant R82A/G231C [J].
Alexiev, U ;
Mollaaghababa, R ;
Khorana, HG ;
Heyn, MP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (18) :13431-13440
[3]   EFFECT OF THE ARGININE-82 TO ALANINE MUTATION IN BACTERIORHODOPSIN ON DARK-ADAPTATION, PROTON RELEASE, AND THE PHOTOCHEMICAL CYCLE [J].
BALASHOV, SP ;
GOVINDJEE, R ;
KONO, M ;
IMASHEVA, E ;
LUKASHEV, E ;
EBREY, TG ;
CROUCH, RK ;
MENICK, DR ;
FENG, Y .
BIOCHEMISTRY, 1993, 32 (39) :10331-10343
[4]   Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsin [J].
Balashov, SP ;
Imasheva, ES ;
Ebrey, TG ;
Chen, N ;
Menick, DR ;
Crouch, RK .
BIOCHEMISTRY, 1997, 36 (29) :8671-8676
[5]   Reconciling crystallography and mutagenesis: a synthetic approach to the creation of a comprehensive model for proton pumping by bacteriorhodopsin [J].
Brown, LS .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2000, 1460 (01) :49-59
[6]   THE RETINAL SCHIFF BASE-COUNTERION COMPLEX OF BACTERIORHODOPSIN - CHANGED GEOMETRY DURING THE PHOTOCYCLE IS A CAUSE OF PROTON-TRANSFER TO ASPARTATE-85 [J].
BROWN, LS ;
GAT, Y ;
SHEVES, M ;
YAMAZAKI, Y ;
MAEDA, A ;
NEEDLEMAN, R ;
LANYI, JK .
BIOCHEMISTRY, 1994, 33 (40) :12001-12011
[7]   Functional roles of aspartic acid residues at the cytoplasmic surface of bacteriorhodopsin [J].
Brown, LS ;
Needleman, R ;
Lanyi, JK .
BIOCHEMISTRY, 1999, 38 (21) :6855-6861
[8]   Functional significance of a protein conformation change at the cytoplasmic end of helix F during the bacteriorhodopsin photocycle [J].
Brown, LS ;
Varo, G ;
Needleman, R ;
Lanyi, JK .
BIOPHYSICAL JOURNAL, 1995, 69 (05) :2103-2111
[9]   GLUTAMIC-ACID-204 IS THE TERMINAL PROTON RELEASE GROUP AT THE EXTRACELLULAR SURFACE OF BACTERIORHODOPSIN [J].
BROWN, LS ;
SASAKI, J ;
KANDORI, H ;
MAEDA, A ;
NEEDLEMAN, R ;
LANYI, JK .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (45) :27122-27126
[10]   RELATIONSHIP OF PROTON RELEASE AT THE EXTRACELLULAR SURFACE TO DEPROTONATION OF THE SCHIFF-BASE IN THE BACTERIORHODOPSIN PHOTOCYCLE [J].
CAO, Y ;
BROWN, LS ;
SASAKI, J ;
MAEDA, A ;
NEEDLEMAN, R ;
LANYI, JK .
BIOPHYSICAL JOURNAL, 1995, 68 (04) :1518-1530