Voltage-dependent closing of porin channels: Analysis of relaxation kinetics

被引:13
作者
Mathes, A [1 ]
Engelhardt, H [1 ]
机构
[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany
关键词
Omp34; Acidovorax delafieldii; ion channel; porin conductivity; voltage gating; Omp32; Comamonas acidovorans;
D O I
10.1007/s002329900416
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
The anion-selective porin Omp34 from Acidovorax delafieldii was unidirectionally reconstituted in planar lipid membranes. Pore closing was recorded particularly at low salt conditions for negative and positive membrane potentials in the range of +/-10 to +/-100 mV. Relaxation curves were fitted by exponential functions in order to describe and to analyze the voltage-dependent behavior. Omp34 exhibited the following characteristics: (i) The channels are asymmetric with respect to closing characteristics and corresponding functional parameters. (ii) Relaxation curves can be fitted by a single exponential function in the low voltage range only, at greater than or equal to 40 mV combinations of two exponential functions are required. (iii) Beyond 60 to 70 mV a third exponential function is necessary to fit the fast closing components properly. The time constants differ by two to three orders of magnitude. (iv) Hysteresis in I-V-diagrams originate from slow relaxation components which are different for positive and negative voltages. The implications for models aiming at description of voltage-dependent closing are discussed.
引用
收藏
页码:11 / 18
页数:8
相关论文
共 31 条
[1]   VOLTAGE-DEPENDENT CAPACITANCE IN LIPID BILAYERS MADE FROM MONOLAYERS [J].
ALVAREZ, O ;
LATORRE, R .
BIOPHYSICAL JOURNAL, 1978, 21 (01) :1-17
[2]   PERMEATION OF HYDROPHILIC SOLUTES THROUGH MITOCHONDRIAL OUTER MEMBRANES - REVIEW ON MITOCHONDRIAL PORINS [J].
BENZ, R .
BIOCHIMICA ET BIOPHYSICA ACTA-REVIEWS ON BIOMEMBRANES, 1994, 1197 (02) :167-196
[3]   Electrophysiological characteristics of the PhoE porin channel from Escherichia coli. Implications for the possible existence of a superfamily of ion channels [J].
Berrier, C ;
Besnard, M ;
Ghazi, A .
JOURNAL OF MEMBRANE BIOLOGY, 1997, 156 (02) :105-115
[4]   FAST AND SLOW KINETICS OF PORIN CHANNELS FROM ESCHERICHIA-COLI RECONSTITUTED INTO GIANT LIPOSOMES AND STUDIED BY PATCH-CLAMP [J].
BERRIER, C ;
COULOMBE, A ;
HOUSSIN, C ;
GHAZI, A .
FEBS LETTERS, 1992, 306 (2-3) :251-256
[5]   CHARACTERIZATION OF THE PORIN OF RHODOBACTER-CAPSULATUS 37B4 IN PLANAR LIPID BILAYERS [J].
BISHOP, ND ;
LEA, EJA .
FEBS LETTERS, 1994, 349 (01) :69-74
[6]   ASYMMETRY OF ORIENTATION AND VOLTAGE GATING OF THE ACIDOVORAX-DELAFIELDII PORIN OMP34 IN LIPID BILAYERS [J].
BRUNEN, M ;
ENGELHARDT, H .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 212 (01) :129-135
[7]   THE MAJOR OUTER-MEMBRANE PROTEIN OF ACIDOVORAX-DELAFIELDII IS AN ANION-SELECTIVE PORIN [J].
BRUNEN, M ;
ENGELHARDT, H ;
SCHMID, A ;
BENZ, R .
JOURNAL OF BACTERIOLOGY, 1991, 173 (13) :4182-4187
[8]   SIGNIFICANCE OF POSITIVELY CHARGED AMINO-ACIDS FOR THE FUNCTION OF THE ACIDOVORAX-DELAFIELDII PORIN OMP34 [J].
BRUNEN, M ;
ENGELHARDT, H .
FEMS MICROBIOLOGY LETTERS, 1995, 126 (02) :127-132
[9]  
BUEHLER LK, 1991, J BIOL CHEM, V266, P24446
[10]   SINGLE CHANNEL BEHAVIOR OF MATRIX PORIN OF ESCHERICHIA-COLI [J].
BUEHLER, LK ;
ROSENBUSCH, JP .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1993, 190 (02) :624-629