Chemoelectrical Energy Conversion of Adenosine Triphosphate using ATPases

Author:

Vishnu Baba Sundaresan 1,Leo Donald J.2

Affiliation:

1. Mechanical Engineering Department, Virginia Commonwealth University, Richmond, VA 23284, USA,

2. Mechanical Engineering Department, Virginia Polytechnic Institute and State University Blacksburg, VA 24061, USA

Abstract

Biological ion transport processes in proteins have inspired the development of bio-sensors, actuators, photoelectric, and chemoelectric energy conversion devices. These bio-inspired devices use ion transport through a protein energized by biochemical reactions in the protein’s sub-units to perform their engineering function. In an effort to advance the use of biological processes in synthetic systems, a chemoelectrical energy conversion device is demonstrated in this article that uses hydrolysis of adenosine triphosphate (ATP) in ATPase enzyme to generate electrical power. The ATPase enzyme in the device is reconstituted in a bilayer lipid membrane (BLM) and supported on a porous substrate. ATP is dissolved in pH7 buffer and added to one of the chambers in this bicameral device. The transmembrane gradient established by proton transport, resulting from hydrolysis of ATP in the enzyme, is converted into electron flow in an external circuit via silver-silver chloride electrodes placed in the buffer solution on both the sides of the membrane. The chemoelectrical energy conversion of ATP is demonstrated in this article using electrical impedance spectroscopy and load characterization experiments on BLMs supported in the pore(s) of a 25% porous polycarbonate membrane and single-pore silicon nitride chip. In electrical impedance spectroscopy, the change in conductance states of the membrane quantified by specific resistance is used to demonstrate protein activity. The mean electrical impedance of the BLM with ATPase supported on a single pore silicon nitride chip drops from 7 kΩ cm2 to 250 Ω cm2 on adding ATP to one side of the membrane. This change in ionic conductance of the BLM with ATPase in the presence of ATP demonstrates protein activity in the membrane. Impedance analysis of the membranes (BLM, BLM with ATPase) supported in multi-pore polycarbonate substrate demonstrates similar trend confirming ion transport and energy conversion in the membrane. In load characterization experiments, a resistive load of known magnitude is connected to the device and voltage across the membrane and current through the circuit are measured. The current−voltage characteristics of the device resembles a constant current power source and the slope of the response represents the internal resistance of the device. The current through the membrane supported on the single pore substrate is below the range of our data acquisition equipment and hence the device with the porous polycarbonate membrane is used in load characterization experiments. This polycarbonate membrane-based device has an open-circuit voltage of 87.5(±7.5) mV with a specific power output of 1.85 μW/cm2 and an internal resistance of 30.5k(±8.5k)Ω. The theoretical maximum specific power available from the membrane supported on the multi-pore polycarbonate membrane and the single pore silicon-nitride substrate are estimated from the current−voltage response to be 7.65 and 18 μW/cm2.

Publisher

SAGE Publications

Subject

Mechanical Engineering,General Materials Science

Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3