Hydrogen Sensing by Enzyme-Catalyzed Electrochemical Detection
- 11 June 2005
- journal article
- Published by American Chemical Society (ACS) in Analytical Chemistry
- Vol. 77 (15) , 4969-4975
- https://doi.org/10.1021/ac050313i
Abstract
Hydrogen (H2) is a possible future alternative to current fossil-based transportation fuels; however, its lower explosive limit in air requires a reliable sensor to detect leaks wherever H2 is produced, stored, or used. Most current H2 sensors employ palladium or its alloy as the sensing element, featuring high operating temperature and limited selectivity. In this study, we report using soluble hydrogenase (SH) of aerobic β-proteobacterium Ralstonia eutropha strain H16 to accomplish ambient, electrochemical detection of H2. Gas samples were collected in a solution containing SH that catalyzed the oxidation of H2. The electrons released during the H2 oxidation reaction were accepted by benzyl viologen (BV2+). The product of the redox reaction, BV+, was then detected using chronoamperometry. Using this sensing scheme, we demonstrate detection of H2 ranging from 1 to 100%. In addition, enzyme kinetics and the effect of oxygen on signal response were studied. Our results indicate that it is feasible to develop a sensor to detect H2 in the atmosphere that is based on enzyme-catalyzed electrochemical detection.Keywords
This publication has 30 references indexed in Scilit:
- The Soluble NAD+-Reducing [NiFe]-Hydrogenase fromRalstonia eutrophaH16 Consists of Six Subunits and Can Be Specifically Activated by NADPHJournal of Bacteriology, 2005
- Structural and Oxidation-State Changes at Its Nonstandard Ni−Fe Site during Activation of the NAD-Reducing Hydrogenase from Ralstonia eutropha Detected by X-ray Absorption, EPR, and FTIR SpectroscopyJournal of the American Chemical Society, 2004
- The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygenJBIC Journal of Biological Inorganic Chemistry, 2004
- Hydrogen-Induced Structural Changes at the Nickel Site of the Regulatory [NiFe] Hydrogenase from Ralstonia eutropha Detected by X-ray Absorption SpectroscopyBiochemistry, 2003
- Functional Analysis by Site-Directed Mutagenesis of the NAD + -Reducing Hydrogenase from Ralstonia eutrophaJournal of Bacteriology, 2002
- Direct and electrically wired bioelectrocatalysis by hydrogenase from Thiocapsa roseopersicinaBioelectrochemistry, 2002
- The NAD-linked soluble hydrogenase from Alcaligenes eutrophus H16: detection and characterization of EPR signals deriving from nickel and flavinJBIC Journal of Biological Inorganic Chemistry, 1996
- Enzymatic conversion of apolar compounds in organic media using an NADH‐regenerating system and dihydrogen as reductantFEBS Letters, 1983
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970