A New Class of Purple Membrane Variants for the Construction of Highly Oriented Membrane Assemblies on the Basis of Noncovalent Interactions

被引:7
作者
Baumann, Roelf-Peter [1 ]
Busch, Annegret P. [1 ]
Heidel, Bjoern [2 ]
Hampp, Norbert [1 ]
机构
[1] Univ Marburg, Dept Chem, D-35032 Marburg, Germany
[2] Univ Siegen, Fak 4, Dept Biol Chem, D-57068 Siegen, Germany
关键词
HALOBACTERIUM SP GRB; MUTATED BACTERIORHODOPSINS; ORIENTATION; PROTEIN; FILMS; TRANSLOCATION; HALOARCHAEA; MOLECULE; MUTANTS; STORAGE;
D O I
10.1021/jp210825x
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070305 [高分子化学与物理];
摘要
Purple membranes (PM) from Halobacterium salinarum have been discussed for several technical applications. These ideas started just several years after its discovery. The biological function of bacteriorhodopsin (BR), the only protein in PM, is the light-driven proton translocation across the membrane thereby converting light energy into chemical energy. The astonishing physicochemical robustness of this molecular assembly and the ease of its isolation triggered ideas for technical uses. All basic molecular functions of BR, that is, photochromism, photoelectrism, and proton pumping, are key elements for technical applications like optical data processing and data storage, ultrafast light detection and processing, and direct utilization of sunlight in adenosine 5'-triphospate (ATP) generation or seawater desalination. In spite of the efforts of several research groups worldwide, which confirmed the proof-of-principle for all these potential applications, only the photochromism-based applications have reached a technical level. The physical reason for this is that no fixation or orientation of the PMs is required. The situation is quite different for photoelectrism and proton pumping where the macroscopic orientation of PMs is a prerequisite. For proton pumping, in addition, the formation of artificial membranes which prevent passive proton leakage is necessary. In this manuscript, we describe a new class of PM variants with oppositely charged membrane sides which enable an almost 100% orientation on a surface, which is the key element for photoelectric applications of BR. As an example, the mutated BR, BR-E234R7, was prepared and analyzed. A nearly 100% self-orientation on mica was obtained.
引用
收藏
页码:4134 / 4140
页数:7
相关论文
共 32 条
[1]
Bending of purple membranes in dependence on the pH analyzed by AFM and single molecule force spectroscopy [J].
Baumann, R. -P. ;
Schranz, M. ;
Hampp, N. .
PHYSICAL CHEMISTRY CHEMICAL PHYSICS, 2010, 12 (17) :4329-4335
[2]
BACTERIORHODOPSIN ORIENTED IN POLYVINYL-ALCOHOL FILMS AS AN ERASABLE OPTICAL STORAGE MEDIUM [J].
CHEN, ZP ;
LEWIS, A ;
TAKEI, HY ;
NEBENZAHL, I .
APPLIED OPTICS, 1991, 30 (35) :5188-5196
[3]
Bacteriorhodopsin-based photo-electrochemical cell [J].
Chu, Li-Kang ;
Yen, Chun-Wan ;
El-Sayed, Mostafa A. .
BIOSENSORS & BIOELECTRONICS, 2010, 26 (02) :620-626
[4]
HOMOLOGOUS BACTERIO-OPSIN-ENCODING GENE-EXPRESSION VIA SITE-SPECIFIC VECTOR INTEGRATION [J].
FERRANDO, E ;
SCHWEIGER, U ;
OESTERHELT, D .
GENE, 1993, 125 (01) :41-47
[5]
MUTATED BACTERIORHODOPSINS - COMPETITIVE MATERIALS FOR OPTICAL INFORMATION-PROCESSING [J].
HAMPP, N ;
BRAUCHLE, C ;
OESTERHELT, D .
MRS BULLETIN, 1992, 17 (11) :56-60
[6]
Bacteriorhodopsin as a photochromic retinal protein for optical memories [J].
Hampp, N .
CHEMICAL REVIEWS, 2000, 100 (05) :1755-1776
[7]
MUTATED BACTERIORHODOPSINS - VERSATILE MEDIA IN OPTICAL-IMAGE PROCESSING [J].
HAMPP, N ;
ZEISEL, D .
IEEE ENGINEERING IN MEDICINE AND BIOLOGY MAGAZINE, 1994, 13 (01) :67-74
[8]
Hampp N., 2004, NANOBIOTECHNOLOGY, P146
[9]
Closing in on bacteriorhodopsin: Progress in understanding the molecule [J].
Haupts, U ;
Tittor, J ;
Oesterhelt, D .
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1999, 28 :367-399
[10]
General concept fur ion translocation by halobacterial retinal proteins: The isomerization/switch/transfer (IST) model [J].
Haupts, U ;
Tittor, J ;
Bamberg, E ;
Oesterhelt, D .
BIOCHEMISTRY, 1997, 36 (01) :2-7